ACA NEWSLETTER - SUMMER 1997

TABLE OF CONTENTS
President's Column
Council News
SIG News
Canadian Division News
Letter to the Editor
E. O. Lawrence Award to Sunil Sinha
Elizabeth Wood Prize to Roald Hoffmann
ACA Publice Service Award to George Brown
Specialist Databases / What's on the Cover
Contibutors/ Exhibitors for St. Louis
Call for Nominations for 1998 Wood Writing Prize
Candidates for 1998 ACA Offices
Hamilton Memorial Scholarship
Pittsburgh Diffraction Society News
Polycrystal Book Service
ACA Corporate Members
West Coast Protein Meeting
Structural Biology Symposium
David Davies Symposium
Mid-Atlantic Protein Meeting
San Diego Continues as NSF Computing Center
CCDC Announcement
Tulinsky Article on the Protein Structure Project
Verner Schomaker (1914-1997)
Calendar of Meetings
Positions Available
ICCD Scholarship

Contributions to the ACA Newsletter may be sent to either of the Co-Editors:

Ron Stenkamp
Dept. of Biol Structure, SM-20.
U. of Washington
Seattle, WA 98195
tel. 206-685-1721
fax 206-543-1524
stenkamp@u.washington.edu

Judith Flippen-Anderson
Code 6030
Naval Research Lab.
Washington, DC 20375
tel. 202-767-3463
fax 202-767-6874
flippen@harker.nrl.navy.mil

Articles by e-mail or on diskettes are especially welcome. Deadlines for newsletter contributions are: February 1, May 1, August 1 and November 1st. Matters pertaining to advertisements, membership inquiries, or use of the ACA mailing list should be addressed to:

Marcia (Vair) Colquhoun, Administrative Manager
American Crystallographic Association
% Hauptman-Woodward Medical Research Institute
73 High Street, Buffalo, NY 14203-0906
phone: 716-856-9600, ext. 321; FAX: 716-852-4846
E-mail marcia@hwi.buffalo.edu

ACA HOME PAGE http://www.hwi.buffalo.edu/ACA/
Contributors to this issue are listed on page 9
ACA Newsletter (ISSN 1058-9945) Number 2, 1997. Published four times per year in the spring, summer, fall and winter for the membership of the American Crystallographic Association, P.O. Box 96, Ellicott Station, Buffalo, NY 14205-0096. Membership in the ACA includes a non-deductible charge of $1.75 from membership dues to be applied to a subscription to the ACA Newsletter. Second-class postage paid at Buffalo, New York. POSTMASTER: Send address changes to ACA, c/o 73 High St., Buffalo, NY, 14203.

PRESIDENT'S COLUMN
I'm writing this column during the last week of classes, the time when my department frantically tries to organize the next academic year before we disperse for various meetings, workshops, conferences and possibly even a vacation. One committee was wrestling with the department's seminar budget, and I feared that a possible casualty would be the general seminar. As its name implies, the general seminar has no special focus, and the topics deal with chemistry, broadly defined. The last three speakers have been a nuclear chemist, a materials scientist, and a biochemist. I needn't have worried about the seminar's future. As one professor put it, "I know what's going on in my specialty, but at the general seminar I find out what's going on in related areas. It's almost the only place now where I learn really new things." In the end, we increased the allotment for the general seminar even though the increase meant cutting our more specialized seminar series.
We all value the opportunity to learn outside of our specialties, and the upcoming annual meeting in St. Louis is a splendid opportunity for such learning. Every time I check the program on the World Wide Web site, I find presentations on topics that I would like to understand but don't. We live in an age when developments in other scientific disciplines very quickly affect our own. For example, there's no doubt that advances in genomics or computational techniques will affect pharmaceutical research, but how? You can get some expert insights in St. Louis. The creative union of ideas from what were once unrelated areas is characteristic of scientific progress, and meetings like the ACA annual meeting are a great opportunity to participate in that process.
Databases are another issue involving the exchange of ideas and information that the ACA, along with many other scientific, governmental and commercial organizations, will be addressing. We're all proud of our community's contributions to some of the world's most useful databases. Crystallographic databases are consulted not only by crystallographers but by medicinal chemists synthesizing new pharmaceutical agents, solid state physicists designing new materials, and computational chemists searching for trends in chemical structure, and many others. Recently databases have been very much in the news, and issues about what information belongs in the database, who owns the data, how databases should be funded, who has access to databases and at what cost, are all being discussed. The issues are complex and contentious, and satisfactory answers will undoubtedly take time and require compromise. The ACA is likely to play a part, albeit a modest one, in the upcoming debates, both as an independent organization and through the IUCr, the USNCCr, and the Committee of Scientific Society Presidents. The fundamental issue is the free and open exchange that is so vital to scientific progress. That free and open exchange requires both a willingness to deposit data and the ready availability of data. The ACA Executive Council will be discussing these issues, and I would encourage interested members to share their ideas.
Finally, the exchange of ideas should involve the largest possible community. Articles in this newsletter describe the Elizabeth Armstrong Wood Prize for promoting a wider appreciation of science and Roald Hoffmann, the first recipient. One of the more pleasurable jobs facing the ACA Executive Council in the upcoming year is selecting the next recipient, and nominations are warmly encouraged.
See you in St. Louis.
Jon Clardy

ACA COUNCIL MEETING, MARCH 1997, BUFFALO, NY
Jane Griffin summarized policies for handling ACA funds. The Finance committee consists of the Treasurer, Financial Advisor and the Past President. Having three people involved is a good protection for the ACA. The Etter Award fund for student travel has grown to the point that the first award for $250 will be given for travel to the St. Louis meeting this July. Bill Duax gave the ACA Headquarters report. St. Louis meeting preparation is going well. A total of 4,487 Call for Papers booklets were distributed to scientists and 438 flyers to potential exhibitors. An electronic version of the Call was placed on the World Wide Web in December, 1996. There will be 53 sessions with 172 invited speakers. Letters of solicitation were sent to ACA members at 90 companies, and commercial donations of $5,100 have been received. Titles and authors of all 452 submitted papers and 100 abstracts have been posted to the Web (as of the time of the council meeting - by press time all abstracts will be on the web). Most abstracts were submitted by e-mail. George Ferguson reported on Canadian issues (see page 7 for his report). Jon Clardy summarized the need for a change in the way we go about choosing meeting sites. Now that the ACA is larger we need to plan further in advance, in order to negotiate for facilities and coordinate meetings with other scientific societies. We may wish to choose a standard site for meetings every third year; this would be more convenient and save money. The Site Selection committee (consisting of the Administrative Manager, Financial Advisor and one ACA member chosen by Council) will routinely choose a meeting site four years in advance. The Vice President will choose the local chair in collaboration with the Site Selection committee; the Vice President will choose the program chair, the symposium topic and symposium chair. The 1997 Membership Directory is in press. It will be sent to those who have paid dues in 1996 or 1997. On next year's dues billing, members will be asked to tick wheter their address information may be posted on the Web. Carol Huber sent a letter to the editors of 37 journals that publish crystallographic results, giving them a copy of the ACA ethics statement. The Council voted by e-mail to support the American Institute of Physics Public Policy Statement supporting increased public funding for science. New representatives to the U.S. National Committee for Crystallography are Jane Griffin (for Carol Huber) and Virginia Pett (for Penny Codding) since Huber and Codding are not US residents. US Congressman George Brown (California) will accept the Public Service Award at the ACA banquet in St. Louis. The Science Writing Award will be named after Elizabeth A. Wood, former ACA president (1957) and author of two books, Crystals and Light and Science from an Airplane Window. The winner of the Science Writing Award is Roald Hoffmann of Cornell University, co-author of Chemistry Imagined, who will speak at the ACA banquet in St. Louis. There will be a notice in the Newsletter asking for nominations for the Elizabeth A. Wood Science Writing Award by October 1 (see p. 13). Nominations should include titles of books and copies of articles. Council will choose the recipient at the October meeting. The Fankuchen lecture will no longer be given at Brooklyn Polytechnic Institute. Rather, in addition to the ACA meeting award ceremony there will be a lecture at the awardee's home institution. Please submit ideas for Physics Success Stories to the committee, which consists of George Ferguson, Louis Delbaere, Steve Ealick and David Cox. The Polycrystal Book Service is for sale. It is one of the benefits of ACA membership and it provides an ACA presence at meetings of other societies. Hauling books to meetings in a van requires energetic and dedicated labor. S. N. Rao met with Mert and Wade Adams in November, 1996. He requested further financial information, and will have recommendations to the ACA Council at the St. Louis meeting.
Virginia B. Pett, Secretary

SIG NEWS
Service SIG Absorption Study
X-ray diffraction studies of compounds containing highly absorbing atoms are often problematic. If the crystal absorbs an appreciable amount of the beam, the data are compromised by an amount which is related to "how much is absorbed", generally determined from the absorption coefficient and the size and shape of the crystal, i.e. the path length for any individual x-ray. Unfortunately, the non-uniformity of the x-ray beam is generally not taken into consideration in these calculations. Various schemes and software programs have been used to "correct" data for absorption, but doubts remain about their effectiveness expecially in cases where the absorption is serious.
Inorganic and organometallic compounds with heavy atoms not only suffer from absorption but also from twinning, superlattice effects, atomic and crystallographic defects, and a host of other problems. In many cases, these structures refine very poorly, a result which is often blamed on absorption but may, in fact, be for one or more of the above reasons. Because we have never been able to obtain routine absorption-free data on these materials, their problems are not often resolved satisfactorily.
With the installation of the Rigaku 2-D image plate system at the APS (designed by Joe Calabrese), DuPont and its DND-CAT collaborators will be able to collect nearly absorption-free x-ray data by tuning to very short wavelengths. One brief data set collected manually using image plates at the NSLS on a crystal of Sr2IrO4 has shown us that the experiment is feasible if tedious. Fortunately, the Rigaku system being installed at the APS is totally automated. A second study at the NSLS on a crystal of Bi4Au2O10 using a Siemens CCD detector with a wavelength of 0.184 Å clearly showed the benefits of using short wavelengths even though the supercell structure has proven elusive.
Not all of our "absorbing" crystals can studied at the APS or at the other synchrotron sources. First, there isn't enough scheduled beamtime or appropriate beamlines to handle all of the potential samples. Second, short-wavelength data collections are limited to materials that have relatively small unit cells. It would thus be useful to have some basis to decide which crystals really benefit from short-wavelength synchrotron radiation and which can/must be done at home institutions with a careful choice of absorption-correction software.
The main purpose of this study is thus to determine which software programs (as a function of crystal size, shape and absorption coefficient) can be reliably used to correct in-house data sets. The plan here is to compare data sets from the APS with those collected and "corrected" in-house. While this study could be carried out alone by DuPont personnel, it would be far more effective (cost/impact/education) if the study could be carried out by a number of Service SIG collaborators who could evaluate all(?) of the computer programs which purport to correct for absorption, comparing the "corrected" data against absorption-free data collected at the APS. The intention is to choose collaborators who have crystals with a wide variety of shapes, sizes and absorption coefficients in order to determine the conditions under which each of the programs is effective and, more importantly, when it is not effective. To help select suitable collaborators, I have set up a committee to review proposed crystals for this study: Ken Haller, Charlotte Stern, Jim Britton. If you are interested in being a collaborator on this project, please provide the following information to Dick Harlow, best reached by e-mail at "harlow@esvax.dnet.dupont.com", who will collect the responses and pass them on to the committee for review. This notice and questionaire will also be posted on the Service SIG webpage (http://www.pitt.edu/~geib/aca.html).
Personal information:
Name, address, phone number, and e-mail address.
Crystal information (more than one can be submitted):
Crystal system, space group, unit cell, formula, m, density.
Description of crystal(s), e.g. shape/habit/faces.
Describe present structural situation:
Type of data collection, e.g. instrument, wavelength, number of reflections, R values, etc.
What's the problem with the present structure? Why is it a good candidate for a short-wavelength study?
Collaboration potential:
What absorption correction programs do you have available, e.g. psi-scan, analytical, artifical (DIFABS)?
It is possible that beam non-uniformity (in-house diffractometers) may also be a major contributor to the systematic errors in the intensity data. You must be willing to measure the uniformity once the most appropriate technique has been established (to be discussed by the collaborators). It may be useful to pass data around among the collaborators to test various correction programs. Can you read/write CIF files?
While it is possible that selected crystals could be sent to the APS for data collection, it is MUCH preferred that the collaborators actually visit the APS and collect their own data (with assistance) since I would like this to be an educational experience for members of the Service SIG. Can you get full or partial support for such a trip to the APS?
Dick Harlow

NAME CHANGE FOR SMALL MOLECULE SIG??
The IUCr Commission on Small Molecules has changed their name to the IUCr Commission on Structural Chemistry. In light of this change, the Small Molecule SIG has been asked to consider changing its name. The officers of SIG invite you to be creative and submit your suggestions for a new name. If you do not think a name change is necessary, let us know that too. Among the suggested names thus far, Structural Chemistry has the majority with Chemical Crystallography a close second. All correspondence should be sent to: Jeanette Krause Bauer Jeanette.Krause@UC.edu FAX: (513) 556-9239 We will be discussing this issue at the upcoming SIG business meeting in St. Louis. An official ballot vote will be conducted later in the Fall.
Jeanette A. Krause Bauer

NEWS FROM CANADA
1. The following good news message was received from Brian Powell (powellb@aecl.ca) concerning the Neutron Program for Materials Research Chalk River Laboratories.
As most of you will already know, finally we have been informed by Minister Anne McLellan that a funding package has been approved to continue operation of the Condensed Matter Science (CMS) program (the Chalk River neutron scattering user program), beyond 1997 March 31. Funding will be provided for three years, with contributions from Natural Resources Canada, the National Research Council, NSERC and Industry Canada. Responsibility for the CMS program will pass from AECL to the National Research Council (NRC) and the program will become part of the Steacie Institute for Molecular Sciences of NRC. A case will have to be prepared by NRC for continued funding beyond the three year bridging period.
The Minister's announcement marked the successful culmination of an intense campaign to save the CMS program, a campaign waged by a huge number of supporters. Without the intense lobbying efforts of our many users, collaborators, friends and allies in many institutions and at many levels, it is doubtful that the government would have been persuaded to reverse its decision to cease funding for the program. NCMS sends grateful thanks to everybody who was involved in the campaign, in whatever role; writing letters of support, talking to M.P.'s, contacting government officials etc. All these efforts were essential in generating enough political support within government to persuade the Minister and her colleagues to find the alternate funding for CMS. Again, thank you to everyone who contributed their time and effort to the "Save CMS" campaign
Now that the threat of imminent termination has receded, NCMS scientists can once more devote their full attention to operating the national user program. In the next two years we must develop and grow the program so that an irrefutable case can be made for continued funding beyond the third year of the bridging period. The spectrometers are all operating, NRU continues to run on a regular schedule and we are open for business. So send in your proposals and come to Chalk River once more to do your experiments. I hope to see you all here in the near future.
2. Cambridge Structural Database (CSD) in Canada
The Department of Chemistry and Biochemistry, University of Guelph, Guelph, Ontario, Canada N1G 2W1, has been chosen to be the National Affiliated Centre for the distribution of the CSD CD-ROM disks to Canadian academic users, effective April 1, 1997. George Ferguson (the Canadian Representative to the ACA Council) will be looking after the details of site-licenses and distribution of disks. If you have not already received a notice about this change and want further information please contact him by e-mail (george@xray.chembio.uoguelph.ca), tel: (519)824-4120, ext 3548 or FAX (519) 766-1499. The April 1997 release of the CSD will be mailed to Canadian site-license holders as soon as the material arrives from Cambridge.
George Ferguson Canadian Representative to the ACA.

THE CANADIAN NATIONAL COMMITTEE FOR THE IUCR
Dr. Suzanne Fortier, Chair
Dept. of Chemistry Queen's University Kingston, Ontario K7L 3N6
phone: (613)545-6933
FAX: (613)545-6934 fortiers@qucdn.queensu.ca

Dr. Isabella Bassignana, Vice-Chair Advanced Technology Lab.
Nortel Technologies
Ottawa, Ont. K1Y 4H7
phone: (613)763-3550
FAX: (613)763-2404
isa@nortel.ca

Dr. Jean-Pierre Charland, Treasurer
DNRC, CANMET,BCC Bldg. 3
Energy Research Labs
555 Booth St.
Ottawa, Ont. K1A 0G1
phone: (613)995-5751
FAX: (613)995-9584
charland@emr.ca

Dr. Joseph Schrag, Secretary
Biotechnology Research Institute
National Research Council of Canada
Montreal, Que. H4P 2R2
phone: (514)496-2557
FAX: (514)496-5143
joe.schrag@nrc.ca

Dr. Francois Brisse
Universite de Montreal
Montreal, Que. H3C 3J7
phone: (514)343-6730
FAX: (514)343-7586
brisse@ere.umontreal.ca

Prof. T. Stanley Cameron
Dept. of Chemistry
Dalhousie University
Halifax, N.S. B3H 4J3
phone: (902)494-3305
FAX: (902)494-1310
cameron@ac.dal.ca

Dr. Randy Read
Medical Microbiol. and Infec. Diseases
University of Alberta
Edmonton, Alta. T6G 2H7
phone: (403)492-4305
FAX: (403)492-7521
rndy@mycroft.mmid.ualberta.ca

Dr. Frank Hawthorne
Dept. of Geological Sciences
University of Manitoba
Winnipeg, Man. R3T 2N2
phone: (204)474-8861
FAX: (204)261-7581
fchawthorn@bldgwall.lan1.umanitoba.ca

Dr. George Ferguson, ex-officio
Chemistry Department
Guelph University
Guelph, Ont. N1G 2W1
phone: (519)824-4120 x3800
FAX: (519)766-1499 george@xray.chembio.uoguelph.ca; ferguson@chembio.ouguelph.ca

LETTERS / NEWS & NOTICES
LETTER TO THE EDITOR - Deposition of Coordinates
I would like to initiate (once again) a discussion about the deposition of macromolecular coordinates resulting from crystallographic investigations of proteins and nucleic acids. For the last several years, virtually all journals publishing macromolecular structures have subscribed to the rules of the Commission on Biological Molecules of the International Union of Crystallography (Acta Cryst. (1989) A45, 658), which require concurrent Protein Data Bank (PDB) deposition of the coordinates, with a possibility of putting them on hold for up to one year (four years for the primary data, such as structure factors or NMR assignments). In most cases these rules are followed faithfully, and even journals which for a long time did not subscribe to them, such as Nature, have now adopted them. However, structures not immediately accompanied by coordinates still get published. Since the latest improvements in the submission process to PDB make it possible to get an accession code almost immediately upon automated delivery of the data, the fault must squarely lie with the authors (and with the journal for not enforcing the rules). Recently, I found papers not accompanied by coordinates in Cell, Nature, Nature Structural Biology, and Biochemistry. Letters written to the editors of the former two journals went unanswered, while the latter two elicited immediate responses, which included contacting the authors of the offending publications and making them deposit the coordinates. It is clear that the journals should be asked to do more to police the rules. If the major journals which publish crystal structures would all agree not to accept any papers from authors who published there previously, but did not deposit the coordinates, then the problem would disappear overnight. I urge the American Crystallographic Association to contact the dozen or so journals in that category, and to suggest such an enforcement mechanism of the existing policy. In addition, if we individually write to the editors when we spot the problem, maybe they will be compelled to act. I feel very strongly, however, that even the current policy has outlived its usefulness and should be changed. The screen of secrecy imposed by the allowed delay in the release of the coordinates is in most cases unnecessary, and often counterproductive. It appears to me that putting crystallographic coordinates on hold is currently becoming a status symbol, aimed only to prove that the deposited structures are really important. How else could we explain that well over half of all structures now deposited with the PDB are placed on hold? The process is rapidly reaching a stage of insanity, with, for example, 19 sets of coordinates of lysozyme currently showing hold status. If there is a justification for this stage of affairs, I fail to see it. On the other hand, I can easily identify many cases when early distribution of the coordinates, even to competing laboratories, has led to great acceleration of investigations, and ultimately benefitted the original team, even if indirectly. The two usual explanations for the need to withhold the coordinates are the desire of the original team to have extra time for full interpretation of their results, or the need to protect commercially valuable information. While the former argument could have been true several years ago, modern methods of structure interpretation make it largely obsolete. The commercial argument is perhaps valid for research supported by companies, but should not be invoked for results of research supported by public agencies. Since the funding agencies, however, have adopted IUCr recommendations, it is unlikely that they will disallow holds unless these recommendations get changed. I would thus like to urge ACA to propose a change in the rules governing deposition of the coordinates, such that the maximum time of the hold would not exceed three months from the date of publication for the coordinates, and 1 year for the original data. This short hold would still allow the authors exclusive time to analyz the results, but would not reduce the papers to mere advertisements, as is currently often the case when the coordinates are not available.
Alexander Wlodawer (wlodawer@ncifcrf.gov)

PROCEEDINGS OF CRYSTALLOGRAPHIC COMPUTING 7 ARE ON-LINE.
After a lot of effort the Proceedings of Crystallographic Computing 7 are on-line. These were the papers presented at the IUCr Macromolecular Computing School last August. They can be viewed at http://www.sdsc.edu/Xtal/IUCr/CC/School96/
Phil Bourne Chairman, IUCr Computing Commission.

1996 EARNEST O. LAWRENCE AWARD IN MATERIALS RESEARCH TO SUNIL K. SINHA
The Lawrence Award was established in 1959 to honor the memory of the late Dr. Ernest Orlando Lawrence who invented the cyclotron and after whom two major DOE laboratories in Berkeley and Livermore, California, are named. The award is given in seven categories for outstanding contributions in the field of atomic energy. Dr. Sunil K. Sinha, a senior physicist at Argonne National Laboratory, was one of the 1996 reciptients of the award.
Dr. Sinha is a leader in the development and use of X-ray and neutron scattering techniques. In particular, he, and his coworkers developed a general theory of X-ray and neutron scattering from "rough" surfaces, i.e., real world surfaces, and then they proceeded to validate this theory by carrying out an imaginative series of experiments. The award citation read: For his wide ranging theoretical and experimental contributions to neutron and X-ray scattering in materials physics; with particular note of his contribution to the development of off-specular surface scattering techniques and their innovative applications to surface transitions in liquid and solid systems, multiple interfaces, thin films, and corrosion processes.
extracted from a DOE news release dated 2/5/97

ACA AWARDS
Roald Hoffmann Awarded the Elizabeth Armstrong Wood Prize
Roald Hoffmann, who is both the Frank H.T. Rhodes Professor of Humane Letters and a Professor of Chemistry at Cornell University, has been named as the first recipient of the Elizabeth Armstrong Wood Prize. The prize recognizes significant achievement in promoting a wider understanding of science.
That Roald Hoffmann survived his childhood was, in itself, remarkable. Before he was four years old, the Nazis forced his family to leave Zloczów, Poland for a Jewish ghetto and then a concentration camp. Smuggled out, he and his mother were sheltered by a Ukrainian teacher who hid them in the attic of a schoolhouse.
After the war, he made his way to the United States, graduating from Stuyvesant High School and Columbia University where he completed his course work in three years and graduated summa cum laude. He earned his Ph.D. in 1962 at Harvard where he then accepted a three-year fellowship. During those years, he worked with Robert B. Woodward, developing what is widely viewed as the most significant recent conceptual advance in theoretical chemistry. In 1965 Hoffmann moved to Cornell University.
Hoffmann's continued erudition has earned him membership in the National Academy of Sciences, The American Academy of Arts and Sciences, and the American Philosophical Society. He is the only person ever to have received the American Chemical Society's awards in three different subfields of chemistry: the A. C. Cope Award in Organic Chemistry, the Award in Inorganic Chemistry, and the Pimentel Award in Chemical Education. In 1981, he shared the Nobel Prize in Chemistry with Kenichi Fukui.
What has made Hoffmann's career most remarkable has been his deep, continuing interest in finding and articulating the connections between science and the arts. He has served as a great popularizer of science not because he oversimplified the technical but because he articulated the complexity of the relationships between chemistry and the rest of human experience. He is also a poet, and his poetry has appeared in a variety of literary magazines and in two published collections entitled The Metamict State and Gaps and Verges. In 1993, the Smithsonian Institution Press published Chemistry Imagined, a unique collaboration between Hoffmann and artist Vivian Torrence. In 1995, Columbia University Press published The Same and Not the Same, a book that focuses on the dualities underlying the field of chemistry. In 1997, W. H. Freeman will publish Old Wine, New Flasks: Reflections on Science and Jewish Tradition by Roald Hoffmann and Shira Leibowitz Schmidt. He has also presented a series of television shows entitled "The World of Chemistry," widely aired on public stations.
Perhaps Roald Hoffmann's greatest contribution has been not in the insights he has achieved in a wide range of fields of chemistry but in his determination to make accessible to everyone the extraordinary links between his beloved science and the worlds of art, literature, and religion.
Jon Clardy

ACA PUBLIC SERVICE AWARD TO THE HONORABLE GEORGE E. BROWN, JR. OF CALIFORNIA
The 1997 ACA Public Service Award goes to Representative George E. Brown, Jr. (D-California) for his very effective service in the cause of science. A graduate of UCLA in Industrial Physics, Brown has been active in science and environmental issues during his more than 30 years in the House of Representatives. He has been a member of the Science Committee since 1965 and is the Ranking Democratic Member of the Committee.
Rep. Brown has been a strong supporter of government funding for scientific research and space exploration. He led efforts in the mid-1960s and again in 1979 to restructure and strengthen the National Science Foundation. He has also sought to open channels of communication between science and government policy-makers by participating in the establishment of the Office of Science and Technology Policy, and the Office of Technology Assessment.
As a concerned and articulate environmentalist, Brown championed the establishment of the Environmental Protection Agency. He has been concerned with carcinogenic pesticides in the food supply, hazards of burning fossil fuels, destruction of the ozone layer and global warming. He calls for a balance between population growth and the use of resources, sustainable development for all members of the world community.
"I know that scientists are uncomfortable with the ethical or moral implications of their work. You tell us that your data is objective, and you leave the value judgments to us. That leaves us free to apply your data in any way we see fit. . . . The time is ripe for a new generation of mythmakers and soothsayers who can help us make the leap beyond narrow self-interest and understand a new reality: that we are all inextricably linked together on this planet, and that the welfare of the whole is of the highest importance. As those with the tools and knowledge to help see the future, scientists have a special and inescapable obligation. Your duty is to speak, not only to the policy makers, but to the world." -Rep. G.E.Brown, Jr. (NATO/Duke workshop on Global Integrated Risk Assessment, 10/95)
Virginia B. Pett

CONTRIBUTORS TO THIS ISSUE
Wade Adams, Jeanette Krause Bauer, Helen Berman, Don Bilderback, Jeff Bolin, Phil Bourne, Susan Chacko, Jon Clardy, Abe Clearfield, Ray Davis, Zygmunt Derewenda, George Ferguson, Steve Geib, Jane Griffin, Dick Harlow, David King, Tom Koetzle, Russ Miller, Virginia Pett, Alan Pinkerton, Ehmke Pohl, Doug Rees, Catherine Schein, Joseph Schrag, Ron Stenkamp, Ken Trueblood, Al Tulinsky, Marcia Vair, Bob Von Dreele, Loren Williams, Alex Wlodawer, Bernie Wuensch, Christine Zardecki. Photos: Bill Duax, Ehmke Pohl, Catherine Schein.

DATABASES / STRUCTURAL INFORMATICS - SPECIALIST STRUCTURAL BIOLOGY DATABASES
One aspect of "Structural Informatics", the subject of this year's Transactions Symposium, is the development of specialist databases called "value-added" or "boutique" databases. These databases combine the information stored in primary archives, such as the Protein Data Bank and the Cambridge Structural Database, with other biological and structural data about the molecules of interest.
The Protein Kinase Resource (PKR; http://www.sdsc.edu/kinases/) is one example of this type of highly specialized resource. The PKR, which is a joint project of the San Diego Supercomputer Center and the Chemistry Dept. of the University of California, San Diego, covers in great detail a single protein family important in signal transduction. Domain experts have formed manual multiple sequence alignments (currently 600 of approximately 1800 known sequences) and family classification based on sequence, structure annotation (currently 32 known structures, excluding model structures), comparison, and conformational analysis. The site also contains general information on investigators, upcoming meetings of interest, and important literature references taken from the OMIM database.
The PKR represents a model for developing a powerful and automatically maintained database and query engine that can be used with a variety of protein families. This on-going work is based on dictionaries for enzymology, sequence features tables, and overall family classification, and is developed in STAR/CIF which complements the existing mmCIF dictionary.
A database dedicated to providing structural information about a single enzyme ‹ HIV protease (HIV PR; http://www-fbsc.ncifcrf.gov/HIVdb/) ‹ has been created at the National Cancer Institute and contains structural data for three PR variants, namely HIV-1, HIV-2, and simian immunodeficiency virus PRs.
The HIV PR database will be the source of all available structures in a unified and fully annotated format. This part of the database, called "Informal," contains information about both the protein and inhibitor present in the complexes of HIV PR, as well as the original sets of coordinates. The information about complexes, PRs, and inhibitors is available separately. Descriptions of the complexes, database-unique labels, PDB names, descriptions of the inhibitors, and references are in the main table which is the gateway between the more detailed information about the PRs, such as the names of viral isolates, and the data on inhibitors. The latter includes chemical formulas, two-dimensional and three-dimensional models, more-detailed description of the compounds, and conditions of the Ki measurements, if available.
The second part of the database, "Analytical," is organized either by services giving access to various tools or by results of specific analyses, which can be viewed immediately. When completed, this part of the database will provide tools for the analysis of the structures which will make it more than just the assembly of the coordinate sets.
One of the first specialist structural databases created is the Nucleic Acid Database (NDB; http://ndbserver.rutgers.edu/). The NDB, which is housed in the Department of Chemistry at Rutgers University, was established to serve as a resource for the nucleic acid community. Data are organized in a searchable relational database that contains not only primary information about the crystallographic experiment that produced the structure, but also derived information about various geometric features. Other features of the NDB include an illustrated atlas of nucleic acid structures complete with crystal packing pictures, bibliographic references arranged according to structural type, and standard dictionaries for nucleic acid components.
The NDB has become a test bed for new database and information technology including the use of mmCIF as its exchange format. More recently, the NDB Project has transferred its technologies for archiving and querying nucleic acid structures to create a more general tool called Protein Finder, that can search for all macromolecular structures. Protein Finder enables the user to search for structures contained in the PDB and to interactively create reports based on the PDB file.
These are but a view examples of the value-added databases that continue to emerge as scientists combine their interests in particular research areas with new computer technologies.
Helen Berman, Phil Bourne and Alex Wlodawer

NEWSLETTER COVER
Credit for the cover goes to Christine A. Zardecki. She is a member of the NDB team at Rutgers University . She assembled the database logos and designed and executed the cover.
The crystallographic community has always been a leader in structural informatics and the databases represented on the cover to do not completely cover what is availabe. The following databases are represented by their logos:

Protein Kinase Resource
http://www.sdsc.edu/kinases/

mmCIF - Macromolecular Crystallographic Information File
http://ndbserver.rutgers.edu/NDB/mmcif/

Protein Finder
http://ndbserver.rutgers.edu/NDB/pfnd-v4/

Molecules R US
http://molbio.info.nih.gov/cgi-bin/pdb/

HIV Protease Database
http://www-fbsc.ncifcrf.gov/HIVdb/

PDB - Protein Data Bank
http://www.pdb.bnl.gov/

BMCD - Biological Macromolecule Crystallization Database
http://ibm4.carb.nist.gov:4400/

CCDC - Cambridge Crystallographic Data Centre
http://www.ccdc.cam.ac.uk/

NDB - Nucleic Acid Database
http://ndbserver.rutgers.edu/

NCBI - National Center for Biotechnology Information
http://www.ncbi.nlm.nih.gov/

MOOSE - Macromolecular Structure Query
http://db2.sdsc.edu/moose/

CATH - Protein Structure Classification
http://www.biochem.ucl.ac.uk/bsm/cath/

NRL_3D - Sequence - Structure Database
http://www.gdb.org/Dan/proteins/nrl3d.html

BioMagResBank
http://bimas.dcrt.nih.gov/sql/BMRBgate.html

Picornavirus
http://www.iah.bbsrc.ac.uk/virus/picornaviridae/index.html

REQUEST FOR NOMINATIONS FOR THE ELIZABETH A. WOOD SCIENCE WRITING AWARD
The ACA Council has voted to name the ACA Science Writing Award the Elizabeth Armstrong Wood Science Writing Award. Dr. Wood is planning to attend the St. Louis meeting to present the award to the first recipient, Prof. Roald Hoffmann of Cornell University.
Dr. Wood was born in New York City in 1912 and received her early schooling at the Horace Mann School of Columbia University. She received her BA from Barnard in 1933, her MA and Ph.D. from Bryn Mawr in 1934 and 1939,respectively, in the area of geology. She joined Bell Research Laboratories in 1943 and remained there until her retirement in 1967. She received honorary D.Sc. degrees from Wheaton College (Mass.), Western College (Ohio), and Worcester Polytechnic Institute. She was President of the ACA in 1957.
The award is being named in her honor for the breadth and clarity of her writing that, in addition to papers in technical journals,includes: Crystals and Light, an Introduction to Optical Crystallography (Van Nostrand, 1964, Dover, 1977); Experiments with Crystals and Light, kit and accompanying booklet (1964 - translated into 6 languages); Crystal Orientation Manual (1963) andScience for the Airplane Passenger (1969 - Japanese Edition, 1972, reissued as Science from Your Airplane Window , 1975).
Nominations of persons who have written books or articles that bring science, especially crystallography or the results of crystallographic studies, to the attention of a wider audience are sought. Successful nominees need not be crystallographers or scientists, and 'writing' could include artistic efforts, museum displays, etc.
Nominations should include the titles of books, copies of articles, or other documentation and should be submitted to the ACA office by October 1. Selection of the winner will be made by ACA Council.

CONTRIBUTORS / EXHIBITORS ACA ST. LOUIS - 1997
We are grateful to the following organizations and institutions whose generous contributions are helping to make the ACA meeting a success.

Boehringer Ingelheim Research Inc.
Bristol-Myers Squibb Pharmaceutical Research Inst.
Charles Supper Company
DuPont Central Research and Development
DuPont Merck Pharmaceutical Company
Enraf-Nonius Corp.
Hampton Research
Hoffman-La Roche
International Centre for Diffraction Data
International Union of Crystallography
Merck Research Laboratories
Molecular Structure Corp.
Oxford Cryosystems
Pharmacia & Upjohn, Inc.
Procter & Gamble Company
Searle
Zeneca Pharmaceuticals

Be sure to visit with our good friends and exhibitors during the meeting.

Area Detector Systems Corp.
Blake Industries
Hecus M. Braun-Graz
Cyberlab, Inc.
Digital Equipment
Diversified Scientific, Inc.
Enraf-Nonius
Hampton Research
Molecular Simulations
Molecular Structure Corporation
National Center for Biotechnology Information
Osmic Inc.
Oxford Cryosystems
PerSeptive Biosystems
Philips Electronic Instruments
Polycrystal Books
Siemens Analytical X-Ray Systems
Silicon Graphics, Inc.
Charles Supper Co.mpany
X-Ray Research GmbH/ Marresearch XRAY Associates

CANDIDATES FOR 1998 ACA OFFICES - SUMMARY

Candidates for ACA Offices in 1998
The Nominating Committee has selected the following candidates for the 1997 elections for ACA offices in 1998.

Vice-President: Abraham Clearfield and Bernhart Wuensch
Treasurer: Jane Griffin

Committees:
Crystal Data & Computing : Russ Miller and Bob Von Dreele
Publications : Douglas Rees and Loren Williams
Apparatus & Standards: Don Bilderback and Alan Pinkerton
Continuing Education : Jeff Bolin and Ray Davis

To nominate write-in candidates for any of these offices write to the ACA Secretary: Virginia Pett, NIH/NIAID, Twinbrook II Bldg, Room 108b, 12441 Parklawn Dr., Rockville, MD 20852 FAX: (301) 402-0284. Letters must be received by September 15, 1997 and must be signed by 5 supporting ACA members and include a signed statement by the candidate describing his or her qualifications. Statements from all candidates will be included with the ballots which will be sent to all members in October 1997.
1997 Nominating Committee, Dick Harlow (Chair), Eddy Arnold and Hugo Steinfink
VICE-PRESIDENT CANDIDATES
Abraham Clearfield
Professor of Chemistry and Director of Materials Science and Engineering Program, Texas A&M University, College Station, TX 77843-3255
Education: BA in Chemistry (1948) and MA in Physical Chemistry (1951) Temple University; Ph.D. in Physical Inorganic Chemistry and Crystallography (1954) Rutgers University.
Professional activities: US National Committee For Crystallography (1992-97), Secretary-Treasurer of USNCCr (1995-'97); Chair Synchrotron SIG (1996), Member Small Molecule SIG; General Chairman ACA Meeting in College Station (1981); ACA Nominating Committee (1992); ACA Awards Committee; Program Director, NSF Structure Program (1972-73); ACA member since 1953; Member ACS, Material Res. Society; ACS Southwest Region Award (1995); Chairman, Southwest Catalysis Society (1994); Chairman, Solid State Subdivision, Inorganic Section, ACS (1984); Workshop on powder diffraction, Univ. de Santandar, Colombia, S.A. (1989); US delegate to Int. Atomic Energy Agency for status of inorganic ion exchangers in nuclear processes (1984); ACS Tour Speaker (1984); Assoc. Ed. Ion Exchange Solv. Extn; Editorial board of 5 journals.
Research interests: Ab initio structure solutions from powder data, solid state and materials chemistry, inorganic ion exchange materials, catalysis.
Statement: As a graduate student I spent the better part of three years to solve two crystal structures. We used Beevers-Lipson strips for structure factor calculations and Pauling punch cards for electron density calculations. Today we could do the job in less than a week. I remember well the first presentation of "Direct Methods" by Herb Hauptman and Jerry Karle and the controversy it stirred. "Put it down in one place (ACA Monograph I) so we can tear it apart at our leisure" was the gist of the arguments. My mentor, Phil Vaughan, one of Pauling's proteges, leaned over and whispered "those guys really are on to something." I'll say! How prophetic those words were. Each decade since then has seen rapid advances in the broad fields of crystallography, structural science and diffraction physics. The advent of high speed computers at modest cost, highly sophisticated software, pulsed neutron sources, high brilliance synchrotrons, image plates and CCD's among other advances have revolutionized our science. Remarkable results have been achieved in the solution of crystal structures from powder data. Widespread application of these powder techniques will be of tremendous benefit to solid state and materials research. The lesson is clear. There are endless frontiers to conquer and our science must remain at the forefront of those frontiers. We can assure this by greater rigor in the training of crystallographers and diffraction scientists. This is particularly lacking in chemistry departments. There is also a need to include more solid state and structural science in undergraduate and graduate programs. As part of our effort in this direction I am organizing a workshop and symposium on "Advances in Structure Determinations" to be held at the Spring American Chemical Society National Meeting in Dallas. The program is sponsored by the Inorganic Division and will mainly be directed towards inorganic chemists. It is especially important that the ACA nurture the new generation of young scientists. Every ffort should be made to provide workshops on special topics, travel funds to attend meetings, and networking opportunities and mentoring by more experienced members. It is most important that we allow them to express their needs to the ACA and that we act on those needs. A major goal of any scientific society is to provide for the professional advancement of its members. As the ACA grows in membership and becomes more diverse we must not lose sight of this goal. We will need to expand the range of our symposia, workshops and special skills training to meet these needs. The ACA has been blessed with very dedicated and farsighted leadership. I would certainly hope to follow in that tradition.

Bernhardt J. Wuensch
Professor of Ceramics, Dept. of Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139
Education: S.B. 1955, S.M. 1957 (Physics), Ph.D. 1963 (Crystallography) MIT
Professional Activities: Member, U.S. National Committee for Crystallography (1980-82, 1989-94); U.S. Delegate, XVI IUCr General Assembly, Beijing (1993). ACA: Program Chairman, Summer Meeting, Boston (1979); Chairman, Warren Award Committee (1981-82); Buerger Award Committee (1984-85); Nominating Committee (1988-89). Mineralogical Society of America: Representative to the ACA (1981 to present). Program Committee, International Conference on Modulated Structures, Kaulua Kona, HI (1979). Co-organizer and Proceedings Co-editor, Neutron Scattering in Materials Science, Materials Research Society (1994-95). Basic Science Editorial Subchairman, J. American Ceramic Society (1970-78). Advisory Editor, Physics and Chemistry of Minerals (1976-85). Associate Editor, Canadian Mineralogist (1979-80); Editorial Board, Zeit. Krist. (1981-88). Fellow: Mineralogical Society of America, American Ceramic Society. Member: ACA, Mineralogical Association of Canada, Materials Research Society.
Research Interests: X-ray and neutron scattering. Inorganic crystal chemistry, sulfides, oxides, and fast-ion conductors. Anharmonic thermal motion. Point defects and mass transport in ionic materials.
Statement: The ACA is presently a robust and vigorous organization. This, I think, is in large measure due to the success of the Special Interest Groups. They have provided effective forums for activities extending across a broad spectrum of the research that constitutes modern crystallography. As a diffractionist working at the juncture of several disciplines, however, I am mindful of the fact that the C that constitutes the middle name of our organization's acronym should always stand for Crystallography in its broadest context; that, in addition to the SIG programs, our annual meeting should continue to support and strengthen Transactions symposia, plenary lectures, and short courses so that we can continue to learn from one another. In similar fashion, I believe that we must continue to vigorously work to strengthen communication and explore new modes of interaction with other societies and groups with interests or techniques that are relevant to the crystalline state. Other issues that raise the level of my adrenalin are criteria for publishing crystallographic data and, especially, the teaching of crystallography (something that I have enjoyed for all of my professional life)‹that our field be communicated broadly, thoroughly, and with authority, for this is an important way in which we ensure the strength and skills of the next generation of crystallographers.

TREASURER CANDIDATE
Jane Griffin
Associate Research Director, Medical Foundation of Buffalo, Buffalo, NY 14203
Education: BA in Chemistry (1954) D'Youville College, Ph.D. in Chemistry (1974), SUNY at Buffalo
Professional Activities: Member US National Committee for Crystallography (1993-1997), ACA, ACS, AAAS, American Peptide Society, Royal Society of Chemistry, British Biophysical Society, Pittsburgh Diffraction Society, AWIS, Editorial Board of J. Medicinal Chemistry. Chair, Direct Methods Meetings (Buffalo, 1976, 1983), Chair, Pittsburgh Diffraction Conference (Buffalo, 1977), Chair, Satellite Meeting of IUCr XII (Buffalo, 1981) Board of Directors, Western New York Technology Development Center (1987- ). Board of Trustees; D'Youville Coll. (1989- ), Nardin Academy (1994- ). Treasurer; Windmill Point Association (1991- ), Women's TAP Fund (1992- ), The Women's Group (1990- ). ACA Activities; Program Chair - New Orleans ACA Meeting (1990), Transactions Chair - McMaster Meeting (1986), Nominating Committee (1979 -1981). ACA Service Award (1991). ACA Treasurer (1994-1997)
Research interests: Structure-activity relationships of steroids, cardenolides, opiates; conformational analysis; CSD database usage.
Statement: It does not seem possible that my first term in office is coming to an end. When I agreed to run almost three years ago I was aware that although the term of the Treasurer was three years, a few Treasurers had served for six years, notably Caughlan, Sparks and Rao. Their generous service to the ACA in that capacity brought continuity not only to that office but also to the Councils on which they served. Dr. Rao continues to provide yeoman service to the ACA as Financial Advisor, member of the Finance Committee and member of the Meeting Site Selection Committee. Because of this shared responsibility, the position of Treasurer is not as burdensome as it was previously. I feel it is an honor to stand for election again

PUBLICATIONS COMMITTEE CANDIDATES
Douglas Rees
Professor, Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125
Education: B.S., Molecular Biophysics and Biochemistry, Yale College, 1974; Ph.D., Biophysics, Harvard University, 1980; Postdoctoral Fellow, Harvard University, 1980-81; University of Minnesota, 1981-82.
Professional Activities: Editorial Boards Science, Protein Science, J. Biological Inorganic Chemistry, J. Molecular Biology. Review Panel, Stanford Synchrotron Radiation Laboratory.
Research Interests: Macromolecular crystallography, especially metallo-proteins and membrane proteins.
Statement: Publications link the present with the future and the past. Not only should publications report current developments, but they must also provide educational and scientific resources for future crystallographers while serving to record past accomplishments. The rapid developments in electronic publishing provide both challenges and opportunities, especially in the areas of crystallographic education and data base management. I would like to work with the ACA to develop these opportunities, while continuing the high quality of our monographs and journals.

Loren Williams
Associate Professor, School of Chemistry and Biochemistry, Georgia Institute of Technology
Education: I graduated from historic Fort Richmond Collegiate in Winnipeg, Canada, which was washed away by the great flood of 1997. I obtained a B.Sc. in Chemistry from the University of Washington in near record time of seven years, and a Ph.D. in Physical Chemistry from Duke University. Post doctoral appointments were at Duke, Harvard and MIT.
Professional Activities: Local Chair, ACA meeting in Atlanta, 1994
Research Interests: DNA damage and serine proteases, intercalation,hydration.
Statement: I encourage everyone to vote for the opposition. If elected I will seek to increase the number of photographs of ACA officers in the ACA newsletter.

CONTINUING EDUCATION COMMITTEE CANDIDATES
Jeff Bolin
Associate Professor, Dept. of Biological Sciences, Purdue University, West Lafayette, Indiana 47907
Education: BS in Biology (1974) Purdue University, MS (1976) and Ph.D. (1982) in Chemistry, University of California at San Diego
Professional Activities: Member of Editorial Board of Journal of Biological Inorganic Chemistry (1995-1997); Member of external advisory committee for the circular polarization beamline resource, ALS, Lawrence Berkeley Laboratory (1993-present); Ad Hoc member of several NIH study sections (1994-1996); Member of: ACS, ACA, Protein Society, Society of Biological Inorganic Chemistry, AAAS, Society of Biological Inorganic Chemistry; Phi Beta Kappa; Big Ten Conference Medal of Honor.
Research Interests: Structure and function of proteins, especially metalloenzymes. Macromolecular crystallography currently centered on non-heme Fe dependent dioxygenases, enzymes with novel metal-sulfur centers, and enzymes involved in processes related to the biosynthesis of such clusters.
Statement: To me, as an experimental scientist, the phrase "continuing education" addresses the efforts we make as individuals to acquire a working knowledge of new methods or procedures pertinent to our research. If I am elected to the Standing Committee for Continuing Education I will be very pleased to work with the leaders of the special interest groups to insure that the workshops associated with our national meetings continue to serve this function over the broad spectrum of our organization.
As a teacher, I believe that "continuing education" should also encompass the means by which we educate others in the fundamentals of our science. Moreover, as a macromolecular crystallographer, I am very much aware that crystallographic research is increasingly accessible to those whose formal education is generally more biological and less physical. And at the same time, the spectacular results achieved by our community emphasize the value of structural studies in biological research. For these reasons, graduate curricula in biochemistry as well as molecular and cellular biology should include units on crystallography. For this reason, I think the Committee should sponsor a workshop in the near future to address the teaching of crystallography in different contexts within graduate and undergraduate life science curricula.

Ray Davis
Distinguished Teaching Professor Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX 78712
Education: B. S. with Honors in Chemistry (1960), University of Kansas Ph. D. in Physical Chemistry (1965), Yale University

Professional Activities: ACA member since early 1960's; Editorial Board, Structural Chemistry, 1989-1991; reviewer for Acta Cryst, JACS, Inorganic Chemistry, Organometallics, Journal of Organometallic Chemistry, and other journals; author of general chemistry textbooks and ancillaries, presently in 5th editions
Research Interests: Continuing education ‹ we are all in that game! The ACA has established high standards for workshops and tutorials, those held in conjunction with ACA meetings and the ACA summer courses, as well as publicizing and supporting other workshops and schools outside ACA. With the burgeoning numbers of highly specialized techniques, both computational and experimental, available not just to crystallographers but also to scientists using crystallography and its results, this kind of face-to-face interaction must be continued in the high-quality ACA tradition. I am sure we will have no shortage of topics on which workshops can be developed.
I believe that ACA should now become more active in the electronic dissemination of continuing education in crystallography. The first and easiest such move is to take on an expanded clearinghouse role in alerting the community to already-existing sites. Each month (week? day?) sees new Web sites on line, so the first and easiest role that ACA could play in this regard would be to expand its present Web-page links to "Products/Service Providers", "Crystallographic Software", and "Other Related Resources". A similar approach could be taken to connect users to educational sites that deal with the teaching of fundamental, as opposed to applied, crystallography. The ACA could also move into the area of developing, or encouraging the development of, an increasing array of electronically available materials. Probably each workshop or tutorial now includes some material that is already, or could be put, in electronic form for Web posting. This electronic availability would make many aspects of the workshops and tutorials available to a much broader audience. Might not some of these efforts overlap similar access available via IUCr or other Internet routes? Of course! But then the approach of "many paths to the same end" is at the heart of today's electronic dissemination of information ‹ and of continuing education.

CRYSTALLOGRAPHIC DATA AND COMPUTING COMMITTEE CANDIDATES
Russ Miller
Professor, Department of Computer Science, State University of New York at Buffalo (SUNY) and Senior Research Scientist, Hauptman-Woodward Medical Research Institute.
Education: B.S. (1980), M.A. (1982), Ph.D. (1985), State University of New York at Binghamton.

Professional Activities: Member of ACA, ACM, IEEE, and IEEE Computer Society. Member of the Executive and Advisory Committees for the IEEE Technical Committee on Parallel Processing (IEEE-TCPP). Co-ordinator for parallel processing education for IEEE-TCPP.
Research Interests: Computational Direct Methods Crystallography, Parallel Algorithms and Architectures, Computational Geometry,Image Analysis.
Statement: As a computer scientist who enjoys collaborative research, I have been fortunate to have worked on several projects (e.g., Shake-and-Bake) with a very talented group of crystallographers and mathematicians at the Hauptman-Woodward Institute. While crystallo-graphers continue to push the forefront of computing, the bulk of their computations are performed on commodity workstations/PCs. However, with multiprocessor machines becoming the standard "departmental" computing engine, one might anticipate that coarse-grained multiprocessor machines, and, in fact, networks of such machines, will soon become a standard computational tool. I would attempt to bring some of my experience in parallel algorithms, supercomputing, software practices, computational science, and web-based computing to the crystallographic community through the efforts of this committee. (http://www.cs.buffalo.edu/pub/WWW/ faculty /miller/)

Robert B. Von Dreele
Staff Member, Manuel Lujan Jr. Neutron Scattering Center, Los Alamos National Laboratory, Los Alamos, NM. Instrument scientist for the High Intensity Powder Diffractometer at MLNSC; developer of the general Structure Analysis System (GSAS).
Education: BS in Chemical Engineering and Ph.D. in Chemistry at Cornell University..
Professinal Activities: Member of the IUCr Commission for Powder Diffraction, Chair-elect of the Neutron SIG, member of ACA, AGU and MSA. co-local chair for the ACA meeting in Albuquerque in 1993.
Research Interests: Powder diffraction data analysis with particular emphasis on Rietveld refinement. In a sense this is my "hobby", namely development of models to describe all the features associated with crystalline materials and how they are manifested in powder diffraction patterns. This includes crystal structure, defects such as micro- and macro- strain effects, texture, diffuse scattering, stacking faults, etc. I am also interested in in situ neutron powder diffraction especially at simultaneous high pressure and high temperature.
Statement: The development of modern computer technology is largely driven by the marketplace interest in user friendly graphical interfaces particularly for desktop workstations and personal computers. The history of computing has been very closely tied to the development of the tools of crystallography for both structure solution and refinement as well as analysis and visualization of the result. However, many of the computer programs readily available to us are no more than adoptions of old mainframe programs written many years ago and they still retain their command driven style of input. I believe that the ACA should strongly encourage the continued development of crystallographic software that makes effective use of the modern graphical interface technology.

APPARATUS AND STANDARDS COMMITTEE CANDIDATES
Donald Bilderback
Associate Director of the Cornell High Energy Synchroton Source, 281 Wilson Laboratory, Cornell University, Ithaca, New York 14853
Education: BS (1969) in physics at Seattle Pacific University; Ph.D. (1975) in solid state physics at Purdue University
Professional Activities: Member: APS, ACA, American Scientific Affiliation, AAAS. Correspondent for Synchrotron Radiation News for CHESS, Technical review committee for Howard Hughs Medical Inst. and for Structural Biology Center for the Advanced Photon Source, Editorial board of Journal of Synchrotron Radiation.
Research Interests: Generating and using submicron hard X-ray beams for microbeam research; better cooling of crystal monochromators under high heat load; micro-Laue diffraction from small crystals; area detectors for X-ray research; and standing wave physics on artificial multilayers and mirror surfaces.
Statement: I am interested to help the apparatus and standards committee with its ongoing work of facilitating interactions between apparatus designers and crystallographic users. Often advances are made in techniques, methods, and equipment design when interested parties have a forum such as the ACA where these concerns can be heard. I have 20 years of experience working at synchrotron radiation sources in the development of x-ray optics, detectors, and crystallographic apparatus that may be relevant for this position and would be willing to serve if elected.

Alan Pinkerton
Professor of Chemistry, University of Toledo. Joint appointment in the Department of Physics and Astronomy. Joint appointment in the Department of Medicinal and Biological Chemistry.
Education: Graduate of the Royal Institute of Chemistry, 1966; Ph.D., Inorganic Chemistry, University of Alberta, 1971.
Professional Activities: Member ACA, ACS, RCS; Local Chair, ACA Meeting, 1991; Chair, Small Molecule SIG, 1994-5; ACA Development Comm., 1989-92; AIP Development Committee, 1995-6.
Research Interests: Small molecule crystallography, experimental charge densities and electrostatic potentials, new crystallographic techniques.
Statement: This is an exciting time to be a crystallographer. The past few years have seen enormous strides in the development of the technology that we use to carry out our work. We can divide these into three general areas - radiation sources, radiation detectors and data analysis. We have witnessed the new generation of synchrotron sources, as well as refurbished or new neutron sources, either coming on line or planned to be so in the near future. In-lab radiation sources have been improved by the introduction of X-ray mirror technology and the future promises the addition of capillary optics. Detector technology has seen the introduction of bigger and better image plates and, more recently, the use of CCD chips. Indeed, CCD devices are rapidly taking over, not only the areas served by scintillation counters, but also the domain dominated by image plates, as phosphors optimized for longer wavelengths and bigger CCD chips, or arrays of chips, come to market. Data analysis for more difficult (read interesting) problems becomes more tractable with the introduction of new and more powerful workstations seemingly on a weekly basis. In parallel to the addition of new hardware, new software is still being produced by the crystallographic community at an astounding rate.
The Apparatus and Standards Committee can serve the community by keeping the membership abreast of these developments. The major tools for this should be the organization of symposia and workshops, both at the annual meetings of the ACA and at sites where the possibility for hands-on short courses exist. For example, the Ohio Crystallography Consortium, which is based at the University of Toledo, would be willing to host a workshop on non-routine experiments using CCD diffractometers, locally developed accessories and expertise drawn from the consortium and from the community at large.
My own crystallographic experience is predominantly experimental, spanning a quarter of a century, two continents and a broad spectrum of hardware and software. There has never been a better time to be a crystallographer whether it be in solid state physics or molecular biology, using in-house equipment or national facilities. Indeed, as we witness crystallization experiments in space, the sky is no longer the limit. I look forward to working with the ACA in keeping our members abreast of the developments in the field and in spreading the excitement that I feel for our discipline as we approach the end of the twentieth century

WALTER C. HAMILTON MEMORIAL SCHOLARSHIPS
Applications are invited for Walter C. Hamilton Scholarships in crystallography for the academic year 1997-98. The Walter C. Hamilton Memorial Fund was established in 1973 under the auspices of Associated Universities, Inc. The Fund is used to provide travel and living expenses for students who wish to come to Brookhaven National Laboratory for limited periods of time (usually no more than about two months) to pursue their research problems using the facilities at the High Flux Beam Reactor or the National Synchrotron Light Source. The Laboratory's facilities are fully available to the students during their stay. To apply for one of the scholarships, the student must submit a research proposal of five pages or less, a summary of his or her educational background (which should include some acquaintance with diffraction techniques), and three letters of reference. These materials should be sent to the Chair, Chemistry Department, Brookhaven National Laboratory, P.O. Box 5000, Upton, NY 11973-5000, and will be reviewed by the W. C. Hamilton Scholarship Committee. Applications for the 1997-98 academic year must be received by August 15, 1997.
Thomas Koetzle

55TH PITTSBURGH DIFFRACTION CONFERENCE
The 1997 Pittsburgh Diffraction Conference will be held 6-8 November, 1997, at the Georgia Center for Continuing Education, University of Georgia, in Athens, GA. Planning is still under way. The conference will consist of two or three symposia as follows: 1. Metalloenzymes, Chair: To be announced; 2. Structured Water, Chair: Loren Williams (GA Tech) 3. Possible third symposium topic to be announced.
This year the Banquet will be held on Friday evening, Nov. 7. The meeting registration fee is $55.00 which includes $5.00 for PDS membership. Tickets for the banquet will be sold separately.
A general poster session will be held in conjunction with the conference. Graduate students are especially encouraged to present their work. A $200 prize in memory of Dr. C.S. Yoo will be awarded to the best poster presentation by a student. Abstracts for the poster session should be sent to S. Geib, Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260. Abstracts must be sent by October 1, 1997.
Nominations are requested for the Sidhu award to be presented during the conference. Nominees should have received their Ph.D after April 1, 1992 and should have a proven record of innovative work in crystallogaphy. Nominations should include at least 2 letters of recommendation along with the nominee's CV, list of publications and reprints of 2 or 3 recent publications. Send nominations to S. Geib before September 15, 1997.
For further information please contact S. Geib (e-mail: geib@pitt.edu. Phone: (412)269-0833). Updated Conference information can be obtained at the PDC '97 Web page at http://www.uga.edu/~biocryst/pdc97.html
Steve Geib

PITTSBURGH DIFFRACTION SOCIETY ELECTION RESULTS
Steven Geib - President-Elect (1997)
Ryonosuke Shiono - Secretary (1997-1998)
Jaime Abola - Treasurer (1997-1998)
Robert F. Stewart - Member-at-large (1997-1998)

S. Swaminathan will serve as PDS President in 1997 and Lavinia M. Wingert will serve as Past-President to complete the Board of Directors.

POLYCRYSTAL BOOK SERVICE
Check out our Website - The "rare" crystallography book auction is finally in full swing! Have you ever wanted to own a first edition Bragg or Friedel?? How about The Precession Method? Or a Vol. I of International Tables?? We'll bring the books to the ACA Meeting in St Louis for delivery to the highest bidders, or ship them if preferred.

NEW BOOKS OF INTEREST TO CRYSTALLOGRAPHERS:
X-ray Charge Densities and Chemical Bonding, by Philip Coppens (Oxford, 358 pages, $85.00 hardbound, 1997) has finally been published! This is Volume 4 of the IUCr Texts on Crystallography, and is the first text "to provide the background necessary for interpretation of the results of accurate crystallographic methods, and to present the concepts to a wider community of nonspecialized scientists." Check our website for a more complete table of contents.
Macromolecular Crystallography, edited by C.W. Carter, Jr. and R.M. Sweet (AP,700 pages, $99.00, 1997) is Methods in Enzymology Volume 276, Part A. Its companion Volume 277 Part B is not due out until early 1998. This volume contains papers on crystal growth, phase determination, instrumentation and data collection, model building, and refinement. According to the authors, these volumes are companions to, not replacements for Methods in Enzymology Volume 114 and 115, which are still available at $179.00 each.
An Introduction to X-ray Crystallography, Second Edition, by M. M. Woolfson (Cambridge, 402 pages, $90.00 hardbound, $37.95 paperbound, 1996) is a textbook for the advanced undergraduate or graduate student beginning serious study of crystallography, and includes all the major topics of crystallography and diffraction. 2-D computer codes are included which enable the student to solve many of the problems included with each chapter.
An Introduction to Hydrogen Bonding, by G.A. Jeffrey (Oxford, 303 pages, $60.00 hardbound, $27.00 paperbound, 1997) is an easy-to-read, well-illustrated and referenced supplement to the brief descriptions of hydrogen bonding found in most textbooks. Its coverage of systems from the weak to the very strong will be useful to those interested in supramolecular chemistry, biological structure and recognition, water and ice, inclusion compounds, and liquid crystals, among others.
The Basics of Crystallography and Diffraction, by C. Hammond (Oxford, 1997, 249 pages, $29.95 paperbound) is IUCr Texts on Crystallography Vol 3, and has just been published! It presents the author's nicely clear renditions of crystallography and diffraction, building on his earlier RMS Handbook. Chapters include: Crystals and Crystal Structures; Two-dimensional Patterns, Lattices and Symmetries; Bravais Lattices and Crystal Systems; Crystal Symmetry, Point Groups and Crystal Structures: the External Symmetry of Crystals; Describing Lattice Planes and Directions in Crystals: Miller Indices and Zone Axis Symbols; The Reciprocal Lattice; The Diffraction of Light; X-ray Diffraction: the Contributions of Max von Laue, W.H. and W.L. Bragg and P.P. Ewald; The Diffraction of X-rays and Electrons; and X-ray and Electron DIffraction of Polycrystalline Materials. Six appendices include model building and kit suppliers, computer programs, biographical notes on scientists mentioned in the text, useful crystallographic relationships, vectors and comnplex numbers, and systematic absences. Answers to problems are included, as are categorized book references. This should prove to be a very popular introductory text!
Total-Reflection X-ray Fluorescence Analysis, by R. Klockenkamper (Wiley, 245 pages, $74.95 hardbound, 1997) overviews the field, compares TXRF to other methods for micro and trace analysis, and describes applications in geology, biology, materials and environmental sciences, medicine, forensics, art history and archaeology.
Dana's New Mineralogy: The System of Mineralogy of James Dwight Dana and Edward Salisbury Dana, 8th Edition, by R. V. Gaines, H.C.W. Skinner, E.E. Foord, B. Mason, & A. Rosenzweig (Wiley, 1997, 1100 pages, $145.00), offers descriptions of all the of the more than 3000 recognized mineral species, emphasizing structure, but also including locations, and has an extensive cross-index.
Introduction to the Theory of Thermal Neutron Scattering, by G.L. Squires (Dover, 272 pages, $9.95 paperbound, 1997 reprint of the 1978 Cambridge edition) is a graduate level text, designed for experimenters who wish to examine the theoretical bases in a relatively informal style, complete with problems and solutions.
Crystal Chemistry and Refractivity, by H.W. Jaffee (Dover, 352 pages, $14.95 paper, 1996 corrected reprint of 1988 edition) covers general principles of crystal chemistry, introduces refractivity, and evaluates crystal structure and bonding effects on optical properties of crystalline materials, with many examples from the major mineral groups.
Symmetry Discovered: Concepts and Applications in Nature and Science, by J. Rosen (Dover, 160 pages, $6.95 paperbound, 1997 enlarged reprint of 1975 Cambridge edition) includes a new preface from the author, solutions to the problems, and an expanded bibliography.
Crystallography, by D. Schwarzenbach (Wiley, 300 pages, $84.95 hardbound, 1997), is a translation from the original French edition by Alan Pinkerton. Provides a thorough understanding of the information contained in crystallographic data files and of the applications of x-ray diffraction methods, describing the background of theoretical and practical aspects from a geometric viewpoint. Numerous figures provide a clear representation of important elements of the subject.
Physical Chemistry: A Molecular Approach, by D.A. McQuarrie and J.D. Simon (University Science, 1200 pages, $76.00 cloth, 1997) Also available, Solutions Manual to Physical Chemistry, 1100 pages, $28.50 paper.
Liposomes in Gene Delivery, by D.D. Lasic (CRC, 320 pages, $59.95 cloth, 1997)
All items can be ordered from Polycrystal Book Service, P.O. Box 3439, Dayton, Ohio 45401, U.S.A., Telephone and FAX 513-223-9070. Prepayment is appreciated, but not required. We will send books with an invoice, and prefer to be paid by check to avoid the service charge from credit card companies. However, charge cards (MC/VISA/AE/DC) are also accepted! Purchase orders are gladly accepted. Please include the appropriate shipping charge: Orders to $20/$4; $20 to $50/$5; $50-$100/$6; $100-$200/$7; over $200 or foreign orders, please inquire. Remember that Polycrystal can order ANY book from ANY publisher ANY time of the year - we distribute for over 200 publishers! Volume and classroom discounts are available.
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MEETING REVIEWS
13th West Coast Protein Crystallography Workshop, Asilomar, Pacific Grove, California, March 15-18, 1997
Sunny California welcomed the more than 300 participants of the 13th West Coast Protein Crystallography Workshop organized by Jim Remington and Wim Hol at the famous Asilomar Conference Center. In addition to a wide range of talks the meeting included two poster sessions and some leisure time for nature walks at the nearby beach. This year's workshop maintained the PI-bar rule continuing its tradition of presentations by young scientists.
The meeting started Saturday night with a session on protein-protein interactions and protein folding. The first structure presented by Nicholas Sauter was the a-lytic protease Pro region that acts as a folding catalyst. Theresa Gamble showed the complex of cyclophilin with the HIV-1 capsid protein. Celia Harrison then presented the heterotrimeric complex of the GrpE and DnaK, and Shankari Mylvaganam reported on her high resolution structures of anti-cytochrome c antibody and its antigen. A highlight of this session was the very entertaining keynote lecture by Roger Tsien. He showed how the crystal structure of green fluorescent protein was utilized for protein engineering.
The Sunday morning session concentrated on receptors and drug design. Richard Wagner showed detailed ligand binding by the thyroid hormone receptor, and Oded Livnah presented the extracellular domain of the EPO receptor complexed with various peptides. The next two talks dealt with T-cell receptor complexes. Chris Garcia described the structure of an T-cell receptor-MHC complex and David Fremont presented structures of T-cell receptors with different ligands. After the coffee break, Mike Randal presented his results on the structure of a high affinity complex between interferon and its receptor. This was followed by Pamela Focia who discussed her results on the structures of the potential drug target HGPRTase. Mary Kopka then presented the crystal structure of the anti-cancer drug di-imidazole lexitropsin bound to DNA, and the session was completed by Susan Hoog who described her structural studies on human herpes virus protease inhibitor complexes.
Kerstin Leuther opened the Sunday evening session presenting her electron microscopy studies on RNA polymerase II-transcription factor complexes which consist of up to 6000 amino acids. The 1.8 Å crystal structure of satellite tobacco mosaic virus using space-grown crystals was described by Steven Larson, and Stefanie Freitag presented crystal structures of wild-type streptavidin-biotin complexes and of a circularly permuted variant. Leemor Joshua-Tor's theme was the role of the C-terminus in the proteolytic activity of the bleomycin hydrolase Gal6. Amy Martin presented kinetic and structural studies on the mechanism of EcoRV endonuclease.
The Monday morning session was dedicated to new methods. Charles Kissinger started with describing a new molecular replacement algorithm featuring an evolutionary search in six dimensions. Susan Heffron described the structure determination of the E. coli EF-Tu:EF-Ts complex by a combination of molecular replacement and multiple isomorphous replacement. The use of Xenon derivatives in the structure solution of hemolin was described by Xiao-Dong Su, and Ed Berry showed the use of molecular averaging over a variety of crystal forms even with protein from different species for bc1 complex crystals. After the coffee break, Thomas Earnest updated the audience about the latest developments regarding two-dimensional pixel array detectors. David Edwards showed how automated map fitting can reduce the amount of time required to interpret a weak electron density map. Jennifer Kelly introduced a novel representation of anisotropic motion in protein crystals that enabled her to model highly flexible loops in neurotropin-3. The presentation by Paul Adams describing the combination of maximum-likelihood and simulated annealing started a lively discussion about general concepts in crystal structure refinement.
There were seven presentations in the following enzyme-mechanism session starting with Andreas Heine who described the mechanism of catalytic antibodies using structures with and without antigen. Ken Goodwill and Christelle Sabatier then shared a double presentation on tyrosine hydroxylase describing the crystal structure and the various inherited diseases associated with mutations of this protein. Next Sarah Gillmor showed the structure of a mammalian 15-lipoxygenase and Catherine Drennan described a complex between vitamin B12 and methionine synthase. Bertram Canagarajah presented the MAP kinase ERK2. The final presentation by Joanne Yeh featured the enterococcol NADH peroxidase and glycerol kinase structures.
The final session of the meeting was dedicated to new crystal structures. Lan Huang led off by describing the structure of the Ras binding domain of RalGDS. Otis Littlefield presented structures of the DNA binding domain of a heat shock transcription factor complexed with DNA. The first structure of a mitochondrial single stranded DNA binding protein was described by Cheng Yang. John Peters presented a novel protein fold in a leucine-rich repeat with a-helices on one side and 310 helices on the other. Andrew Huber discussed the armadillo repeat region of b- catenin. This 540 residue structure was solved using MAD data from 16 selenomethionines. Lesa Beamer presented the human bactericidal/permeability-increasing protein that consists almost entirely of b-sheets. Rhett Kovall presented the crystal structure of a new lambda exonuclease. The final talk of the meeting was given by John Tesmer describing his results on the structure of RGS4 complexed with Gi1, where AlF4- was used to mimick the transition state of the phosphoryl transfer reaction.
Ehmke Pohl

STRUCTURAL BIOLOGY SYMPOSIUM OF THE SEALY CENTER FOR STRUCTURAL BIOLOGY GALVESTON, TX, APRIL 11-13 , 1997
Over two hundred scientists, more than half of whom presented posters, attended the second annual symposium. All the speakers, attendees, and sponsors noted that the spirit and the hospitality of the meeting were wonderful, a tribute to the chairman, Werner A. Braun, and the other organizers, particularly James Lee and Shirley Broz. The symposium began with a presentation of a crystal whale (sperm whale myoglobin was the first protein to yield to X-ray crystallographic analysis) to Dr. Thomas James, president of the UTMB Galveston, for his support of structural biology. In accepting, Dr. James revealed that the shape was especially appropriate, as he used whale heart for his studies on heart muscle function.
This remembrance of the origins of structural biology was a pleasant start to a varied and challenging series of lectures in experimental determination of macro-molecular structures and recognition, computational methods, and protein design. In the keynote address, James Wells of Genentech showed how high resolution X-ray and NMR structures of protein complexes (human growth hormone (hGH), Staph protein A, atrial natriuretic peptide) allowed one to select smaller and cheaper molecules for the same function. Phage display technique yielded hGH mutants that bound to a receptor in which a tryptophan side chain critical for tight binding of the hormone was mutated. In the long term, this technique could select "customized hormones" to activate mutated receptors unable to respond to normal hormones, or binding inhibitors where the receptor is overstimulated (e.g. acromegaly). High resolution structures of protein complexes and how to use the information from them was the theme of several other talks. Johann Deisenhofer of the UT-Southwestern Medical Center, Dallas received the chemistry Nobel prize in 1988 with Hartmut Michel and Robert Huber for solving the structure of the photosynthetic reaction complex. He described the crystal structure of an even larger membrane complex, mitochondrial ubiquinol: cytochrome c oxidoreductase. Among the more fascinating aspects was an internal cavity which he hypothesized could be a storage site for hydroquinone reduction and recycling, thus keeping the substrate from diffusing away.
Lorena Beese, of Duke University Medical Center, presented a "high resolution snapshot of a polymerase in action". Extremely accurate structures allowed her to observe DNA replication by a thermophilic DNA polymerase within the crystal lattice.
Robert Fletterick, University of California, San Francisco (UCSF), summarized a class of molecules he calls "the cell's motors", nucleotide driven proteins that power transport within the cell. The overall similarity of the proteins is best seen at the tertiary level, e.g., the crystal structure of kinesin linked it to an apparently dissimilar muscle motor, myosin. The role of computational chemistry in macromolecular structure determination and prediction was also emphasized. Irwin Kuntz of UCSF showed examples where structure based molecular design was used to design drugs and enzyme inhibitors. He has a revised program, DOCK 4.0 which can be downloaded from the Internet which "docks" a molecule to another using a simple graphics matching algorithm, and a new program "BUILDER", where a small molecule can "grow" within the desired site. Serge Timasheff, professor emeritus of Brandeis University, discussed the binding of salts and osmolytes to proteins in mathematical terms. A practical theory for the interaction of co-solvents specific proteins should aid in obtaining high concentration protein solutions needed for obtaining crystals and NMR analysis.
David Eisenberg (UCLA) presented a new interpretation of oligomer formation, " domain swapping". Several crystal structures show two monomers (e.g., Diptheria toxin) exchanging a segment when forming a dimer. The requirements are a large area of the protein with clear hydrophobic and hydrophilic faces joined to the rest of the molecule by a flexible linker. The mechanism can account thermodynamically for why aggregates form more easily once a dimer forms, and why it is difficult to separate aggregates.
George Georgiou, of the UT-Austin, has a bacterial cell surface expression system for engineering antibodies, which exposes the mutated protein to solution with unrestrained flexibility. He also has an in vitro automated selection system, where mutated DNA is transcribed with T7RNA polymerase, the mRNA is translated in a lysate and selection of proteins based on their ability to bind hapten is done robotically. Stan Watowich (UTMB Galveston) presented ongoing crystallographic studies of kinases involved in intracellular signal transduction. David Gorenstein (UTMB, Galveston) showed the 750 MHz NMR structure of two conformers of Benzo[a]pyrene Diol Epoxide/DNA adduct which in one conformation is highly carcinogenic and suggested aspects of the structure that may account for toxicity. Kathleen Matthew (Rice University, Houston) has combined site-directed mutagenesis studies with molecular modeling and analysis of the crystal structure of the lac repressor protein. Mutants that retained full inducer (IPTG) and receptor binding but adapted a dimer rather than a tetramer structure were made by altering a few critical amino acids. Even a high resolution structure cannot explain everything, however. In an amusingly presented talk, Michael Weiss (University of Chicago) showed that removing structure from the transcription factor SRY made it bind more specifically to DNA. Two point mutations in the DNA binding region rendered the NOESY spectrum of the free protein esssentially peak-less in that area, while that with DNA was as clear and structured as for the wild type complex. This "battered protein" (Weiss compared what they were doing to smashing a piano to improve tone), unlike its parent, did not bind non-specific DNA, although both proteins complexed irreversibly with their substrate and were able to bend DNA. Discussion continued at the poster sessions, which ranged from new computational methods to describe the surface area of molecules (group of Werner A. Braun) to crystal structures of proteins at < 1 ‰ resoltion from Kurt Krause's group at the University of Houston. We hope that the spirit will continue in next year's symposium (see our web site http://www.scsb.utmb.edu for information).
Catherine H. Schein

SYMPOSIUM IN HONOR OF DAVID R. DAVIES' 70TH BIRTHDAY, NIH, APRIL 25, 1997
David was born in Wales and studied at Magdalen College. He obtained his D.Phil from Oxford University, and was a postdoc in Linus Pauling's laboratory at Cal.Tech before coming to the NIH in 1955. He has been and is currently involved in a vast variety of novel structures and structural analysis studies. Postdocs from his lab have gone on to found four independent crystallographic groups at the NIH, and many laboratories in academia and industry.
The symposium was opened by Philip Gordon, Director of NIDDK, and the first session was chaired by Kiyoshi Mizuuchi. Brian Matthews (U. Oregon), a former postdoc of David's, described the work of his laboratory on T-4 lysozyme as a model system for examining protein stability and folding. Residues in highly mobile sidechain regions were generally substitutable by other amino acids, while those in the more rigid parts of the molecule were very sensitive to mutation. Insertions into helices caused translocation rather than local bulges. Studies of interior cavities led to recent experiments with rare gases diffused into the protein. Definite difference peaks were observed, with weak peaks indicating either weak binding or fewer electrons. Multiple methionine substitutions still maintained the three-dimensional structure and activity. He likened the structure of T-4 lysozyme to a 'tolerant jigsaw' model.
Alex Rich (MIT), who first invited David to work at the NIH in 1955, spoke about Z-DNA and MRNA editing. Their collaborative work in the early 60's was the first to show regular RNA structures with complementary strands. He discussed Z-forming sequences, which form Z-DNA but are relaxed back to B-form DNA by topoisomerases in a short time. RNA adenosine deaminase, which unwinds double-stranded RNA but not DNA or single-strand RNA, has been extensively studied by his laboratory.
Michael Potter's (NCI) talk followed, entitled 'Pathogenetic mechanisms in plasmacytoma development'. After describing David as the 'Renaissance Man of Structural Biology', he gave a fascinating history of the early discovery and production of monoclonal antibodies. McPc603 was the first myeloma protein with known binding specificity (to phosphocholine) to be structurally characterized. This protein has gained new interest with the recent discovery by Martin Young that the antigen specific for McPc603 is a carbohydrate from Proteus morganii, a bacterium. Recent work by Matthew Scharff and coworkers showed that a single-site mutation in S107, another antiphosphocholine autoantibody, abolishes its phosphocholine specificity but acquires binding to double-stranded DNA.
The morning session concluded with a talk by Gary Felsenfeld, a longtime fellow scientist with David at the Lab of Molecular Biology, NIDDK. His talk, 'Chromatin Structure and Gene Expression' described the simplest chromatin structure as 'beads on a string' separated by linker DNA. The nucleosome beads, 165 bp DNA wrapped around histone octamers, are further compacted into fibers. The transcriptionally active sections are still partially compacted. Promoter and enhancer regions are relaxed and lose the histones, and supercoiling is positive ahead of transcription and negative behind. Recent data shows that the transcribed end reuses the same histone octamer.
After lunch, Bill Eaton of NIDDK took over as session chair. The first talk of the afternoon, by Edith Miles (NIDDK), described the structural studies of the tryptophan synthase complex, a collaboration between her lab and David's. Early studies of this complex produced in E.Coli did not crystallize, but (10 years later!) protein from Salmonella produced well-diffracting crystals. The a2-b2 tetramer showed that the active sites in the a and b subunits are 25 Åapart, but that a hydrophobic tunnel provides a physical conduit for indole channeling. Recent high resolution studies of mutant enzyme with and without bound ligands to the a and b subunits have provided details about the catalytic and allosteric properties of the enzyme.
Marty Gellert, another founder and current member of LMB, NIDDK, discussed VDJ recombination. The first step is a site-specific cleavage which generates one hairpinned and one blunt-cut coding end. RAG1 and RAG2 proteins are required, and interestingly, can transfer VDJ activity to non-lymphoid cells. The cleavage step involves nicking and hairpin formation, for which a divalent ion is required. With Mg++, the reaction stops after the nicking, while with Mn++ it continues to completion.
'Cooperative folding of an apo-myoglobin folding intermediate', was the title of Robert Baldwin's (Stanford) talk. NMR spectra of partially unfolded proteins were shown to have features of both fully folded and fully unfolded states; thus, they were folded in regions. Intriguingly, studies by Schulman and Kim on a-lactalbumin have shown exactly the opposite result! Baldwin's group has also looked at mutants involving solvent-exposed residues, and concluded that destabilizing mutations lead to non-cooperative folding. Cooperative folding has been shown to depend on stability and the action of some salts.
Ira Pastan (NCI), another collaborator and tennis partner of David's from NIH, spoke about the design and testing of recombinant immunotoxins in human cancer. The toxin used was Pseudomonas exotoxin A, which kills cells by interfering with the ribosomal machinery. The second and third domains of this toxin were attached via a lysine to the B3 antibody, whose antigen is a carbohydrate highly expressed in many cancers. This immunotoxin was put into clinical trials with significant success, but it was discovered to have a long half-life and to cause damage to epithelial cells. A refined version had the variable domains of the antibody as a single chain, and had a shorter half-life but was susceptible to aggregation. A disulfide-stabilized Fv made by mutating two residues to Cys was much more stable and is currently in clinical trials.
Paul Sigler (Yale) described his learning experience as a postdoc in David's lab, and went on to discuss 'Trimeric G proteins: Structure, mechanism and regulation'. He described G-protein mediated transmembrane signalling, focusing on transducin and its signalling action in the retina. The a subunit of this 3-domain protein has been solved in complex with a GTP analog, GDP and GDP+AlF4.. The b and g subunits were solved independently, as well as in complex with GDP and a GTP analog. This family of structures showed that the GTP-GDP change was accompanied by three loop movements, and identified a possible membrane-binding surface.
Returning to the origins of protein crystallography, Max Perutz (MRC, Cambridge) closed the symposium with 'How the structure of proteins was not solved'. He described the intellectual excitement at Cambridge starting in the 30s, with photographs of John Bernal, Dorothy Crowfoot (later Hodgkin) and W.L. Bragg in those days. During the early days of his work on hemoglobin, solving the structure of a protein was considered a hopeless task by many crystallographers. He traced the breakthroughs in the diffraction analysis, mostly done by hand and eye in those days before computers were commonly available. Once it was determined that a heavy atom crystallized along with the protein could be detected in the diffraction pattern, the structure was deemed solved. (Michael Rossman followed this talk with an anecdote: at the time he was considering working with Perutz, another crystallographer told him 'You know, what Max does is not really science'!)
The symposium was followed by a banquet at the NIH Cloisters, enlivened by reminescences from Brian Matthews, Paul Sigler, Alex Wlodawer, Rick Bott, Sally Davies, Gary Felsenfeld, and Marty Gellert. Summaries and photographs of the symposium will be at http://www-mslmb.niddk.nih.gov/davies70/
Susan Chacko

THE 27TH MID-ATLANTIC PROTEIN CRYSTALLOGRAPHY MEETING , MAY 8-10 , CHARLOTTESVILLE, VIRGINIA.
At the start of the meeting we were reminded that it was in Charlottesville that Bob Kretsinger organized the first MPCM and that in those days all the participants could easily fit in Bob's living room. Attendees also had the opportunity to visit the new crystallographic lab in the Health Sciences Center at UVa, recently established by Wladek Minor, Fraydoon Rastinejad, Michael Wiener, Ulla Derewenda and Zygmunt Derewenda, all of whom served on the Organizing Committee with Bob Kretsinger and David Benjamin; Wladek Minor ably chaired this body.
The Meeting had a record number of 151 registrants, and some speakers, specifically George Sheldrick, Eleanor Dodson and Jorge Navaza, flew from locations not typically associated with the US East Coast. The meeting opened on Thursday, May 8, with a keynote address by Paul Sigler. His talk, a Jessie Beams Memorial Lecture in Biophysics, was co-hosted by Tom Thompson, chair of the Biochemistry Department at UVA. Paul talked about the mechanisms of signal transduction by trimeric G-proteins. The picnic which followed was somewhat affected by the weather, but the discussions provided extra heat.
Friday was packed with seventeen 20 min presentations, addressing either structural studies of vital proteins or some aspects of crystallographic methodologies. The session was co-chaired by Bob Kretsinger and Zygmunt Derewenda. It is somewhat unfair to highlight any of the presentations­all were very good­but it may be informative to mention a few, though arbitrarily selected. Jim Hurley, NIH, spoke about the structure of the homodimer of the catalytic subunit of adenylyl cyclase, one of the critical effectors of trimeric G-proteins. Michael Word, Duke University, presented results of packing analysis in high resolution protein crystal structures, an analysis facilitated by a new software package developed at Duke. The approach involves van der Waals contact analysis only after calculated positions of hydrogen atoms are included. Several errors in high resolution structures were identified, many including Asn and Gln residues. Jacek Lubkowski, NCI Frederick, spoke about complexes of L-asparaginase with inhibitors and presented evidence implicating Thr12 as a nucleophile, while Osnat Herzberg introduced an interesting hypothesis of domain rotation that attempts to explain the mechanism by which remote sites in pyruvate phosphate dikinase communicate.
There were a number of posters on display and the individuals presenting them had an opportunity during the Friday session to introduce themselves and describe their posters in a couple of sentences. The challenging day was crowned by another picnic, this time featuring fine steaks and a splendid evening.
Saturday was a real treat. If you are close to the East Coast and you missed it, you have yourself only to blame (at least watch out for next year's Meeting). Two workshops running in parallel focused on data collection and refinement. The former workshop included Zbyszek Otwinowski (Southwestern, Dallas) and David Rodgers (University of Kentucky); the latter included George Sheldrick (Göttingen, Germany), Eleanor Dodson, (York, UK) and Jorge Navaza (Paris, France).
During the refinement workshop, chaired by Fraydoon Rastinejad, George Sheldrick described in detail the new version of his SHELX97 suite (http://linux.uni-ac.gwdg.de/SHELX) which is particularly aimed at those macromolecular aficionados who regularly abused earlier versions. The refinement suite now features a selection of routines that integrate it with other packages, such as the CCP4. The program includes a classical Fourier summation and is intended specifically for high resolution structures, i.e. ~1.7Å or better. Its features include anisotropic treatment of displacement (B) parameters. Two questions are most commonly asked here: at what resolution should one start to use the anisotropic model, and how much time does this refinement really take? George had answers to both. Meaningful anisotropic refinement has been reported using data to 1.5Å or higher, although typically these data were of very high quality, i.e. complete and with high I/s(I) ratio even in the outermost shell. The free R factor is a useful monitor and should decrease at least by 1%, preferably more, to validate the calculation. You can keep the same set of free reflections as you go from X-PLOR to REFMAC and SHELX, so that the latter can be used only in the final stages of work. The results should be chemically meaningful and one should see typically main chain carbonyl oxygens vibrate perpendicular to the peptide plane, etc. Finally, the issue of time. Owing to Wladek's energy George was able to carry out his bench test (1 cycle, 400 atoms) on a 433MHz Digital ALPHA workstation: 63 seconds. This is twice as fast as on a DELL PC with Pentium Pro­standard in George's laboratory­although there will soon be a version for a dual processor PC. It is also four times faster than on the SGI Indigo 2. One should note that PC under the Linux operating system constitutes an increasingly attractive option as a number-cruncher in a crystallographic laboratory.
Eleanor Dodson expanded in her presentation on the use of REFMAC, the maximum likelihood refinement package that is now a part of the CCP4 suite (you can ftp the new suite from ftp.ccp4.db.ac.uk). Eleanor started with a show of 'Fourier ducks' that suffered from various mutilations in the original transform. Note that these and similar images can be found in Kevin Cowtan's Picture Book of Fourier at http://www.yorvic.york.ac.uk/~cowtan/fourier/fourier.html). In this way we were shown how incomplete data affect our electron density maps, and how this is dependent on exactly what data (a shell, a cone, random, etc) are missing. These diagrams­as Eleanor suggested­ should really be on the wall of every X-ray lab, as a permanent reminder of how a good experiment ought to be conducted. The REFMAC program has numerous advantages. Because the minimized quantity is different from that in classical least-squares, the resulting estimates of phase angles coupled with the sA weighting lead to electron density maps of superior quality. It has also been found that the resulting agreement between calculated and observed amplitudes is frequently better. Eleanor also described the problem of anisotropy in the data, often encountered with flash frozen crystals. REFMAC offers the possibility of anisotropic scaling which frequently reduces the conventional R factor by several percent.
Jorge Navaza discussed new ideas that are being implemented in AMORE, the revolutionary Molecular Replacement suite that solved many problems that have aged confined to the depths of our drawers while awaiting their luck. We looked with amazement at the high-tech screen in the auditorium which let us see the screen of the SGI monitor that Jorge used to demonstrate his software. As the molecules moved around the screen to fit within a unit cell without colliding with one another, real-time R factor and correlation factor calculations monitored the likelihood of the solution. His presentation precipitated a discussion on validation of MR solutions: the consensus seemed to be if in doubt, get independent phasing information.
Finally, Xinhua Ji discussed the difficulties in refining flexible fragments of the structure. One of his comments, reiterated by both George and Eleanor, was that one should use all data and not truncate or otherwise mutilate your experimental results. When dealing with weak data, it often pays off to recollect, using longer exposures, higher flux sources, etc.
Questions and open discussion lasted for over 90 minutes after lunch, demonstrating the need for such training events and hunger for knowledge among our young colleagues. It was invigorating to have been a part of this debate and George Sheldrick said something very similar to Wladek as he boarded his plane on Sunday morning.
A workshop on "Cryo-crystallography and Data Collection," attended by 35 people, was chaired by Michael Wiener (UVa). David Rodgers (U. of Kentucky), who is in his words "the only protein crystallographer in the state of Kentucky," presented a lecture on cryocrystallography. David, who has written the "Practical Cryocrystallography" chapter in the new Methods in Enzymology volume 276 (Macromolecular Crystallography, Part A), has developed a variety of technical methods as well as set much of the oral tradition of cryocrystallography into print. Topics included a brief history of the method, cryosolvent selection and crystal transfer/handling, and display of a variety of essential widgets for use of the methods. A lively discussion of the use of liquid N2 versus propane for rapid cooling took place, with a decidedly partisan group advocating the use of liquid N2 However, David presented data from T.-Y. Teng (inventor of the loop-mounting method) on rates of cooling for different methods, indicating that liquid propane may cool samples somewhat faster than liquid N2 . A handy tip: if your crystals are drying out rapidly in the loop after mounting, place a humidifier nearby to increase the relative humidity a bit.
The inimitable Zbyszek Otwinowski (UT Southwestern) followed with a lecture on data collection and reduction, centering around (surprise!) an exposition on the use of the DENZO/SCALEPACK software package. The autoindexing continues to be made increasingly robust. Among other features, the "FIT ALL" command is actually now a smart command, which will only fit those parameters appropriate for the indicated detector and resolution of the data. Data consisting completely of partial reflections can also be handled. Also, aspects of a very nice GUI (graphical user interface), which promises to be a wonderful front-end for use of the software, were presented. Some of the underlying theoretical issues were also presented, chiefly the use and importance of error models for appropriate statistical validation of data reduction. There was a spirited diatribe regarding the uses and abuses of the Rsym statistic to make data appear of nearly arbitrary quality in a user-dependent fashion, and the advocacy of I/s(I) as a better indicator of data quality (along with essentially no intensity cutoff for data reduction). Following the lecture, interested individuals accompanied Z.O. for further hands-on work.
Many participants expressed their regrets that it was not possible to attend both workshops. Indeed, with hindsight, we should have probably organized parallel structural sessions on Friday to allow for workshops to be run consecutively. Maybe next year the organizers will take this option into consideration.
The Meeting was made possible by generous support of sixteen sponsors, many of whom exhibited their products during the meeting. Next year, we will all assemble again. Watch out for the news!
Zygmunt Derewenda & Michael Wiener

NEWS & NOTICES
San Diego Supercomputer Center to Continue Support of Crystallography
The San Diego Supercomputer Center (SDSC) is to become the leading edge site in a National Partnership for Advanced Computing Infrastructure (NPACI) headed by the University of California, San Diego (UCSD). SDSC will receive funding for at least the next five years from the National Science Foundation (NSF) as one of the country's two major centers for high performance computing. The other is the National Center for Supercomputing Applications (NCSA).
Part of the mandate for SDSC is a teraflop/petabyte initiative. In the short term SDSC will receive the first TERA computer expected to perform at over 1012 floating point operations per second. At the same time massive handling in the 1015 byte range is being designed and implemented.
SDSC supports a number of initiatives in crystallography (see http://www.sdsc.edu/Xtal/Xtal.html), including software development and the activities of the ACA and the IUCr. These initiatives will be expanded in the next five years. Suggestions from the community as to the type of activities we should support are welcome and can be sent to bourne@sdsc.edu.
Phil Bourne

CAMBRIDGE CRYSTALLOGRAPHIC DATA CENTRE (CCDC) ANNOUNCES NEW APPOINTMENTS
The Board of Governors of the CCDC has made two key appointments to secure the future development of Centre in sucession to Dr. Olga Kennard, OBE FRS. They have appointed Dr. David Hartley as Executive Director. He will be responsible for the overall management of the Centre, and will contribute considerable expertise to the development of the informatics infrastructure of the CCDC. He was director of the University of Cambridge Computing Service from 1970 - 1994. Since then, he has been Chief Executive of the UK Education and Research Networking Association which is reponsible for the develpment of JANET and SuperJANET networks.
The Board has also appointed Dr. Frank Allen as Scientific Director of the CCDC. Dr. Allen will be responsible for the scientific strategy of the Centre. He joined the CCDC in 1970 and was appointed Deputy Director in 1992. He is well known for his contributions to the development of the CSD System and for his research work in structure correlation and chemical information science. He has a strong background as an academic crystallographer, being a member of the IUCr Committee on Crystallographic Databases, Editor of Section B of Acta Cryst, and Vice-President elect of the British Crystallographic Association.
The two appointments are designed to enhance CCDC's unique position within the international scientific community and to strengthen its information systems development, support and distributions capabilities.
David King

THE PROTEIN STRUCTURE PROJECT
The Protein Structure Project is the topic of a fantastic, very readable article by Al Tulinsky published in Annual Reports in Medicinal Chemistry (1996) 31, 357-366. David Harker, when Irving Langmuir asked what he'd do with a million dollars, stated he'd solve the structure of a protein. In 1950, Langmuir finished raising the funds, and Harker organized a group to solve the structure of ribonuclease. It's interesting to have a first-hand account of how various technical problems were solved, things like crystal growth, making and using isomorphous derivatives, diffractometry, and computing. Many of the techniques now in use in daily structure determinations, both macromolecular and small molecule, stem from the Protein Structure Project. Harker and friends deserve great admiration and credit for their efforts and creativity. Tulinsky presents the issues and problems faced by the Project in ways that make them exciting 45 years later. Reprints of the article are available from Al Tulinsky, Department of Chemistry, Michigan State, East Lansing, MI 48824-1322

VERNER SCHOMAKER (1914-1997)
Verner Schomaker, possessor of one of the most critical and wide-ranging scientific intellects of our time, died in Pasadena, California, on March 30, 1997, of pancreatic cancer. What follows is a very personal account. Many of those who worked with or were closely exposed to Verner might have written something similar; I am confident that the general flavor would have been the same.
Every scientific question seemed to interest Verner, and anyone with a knotty problem was welcome at his always-open door. And his time was always yours ‹ until he, at least, understood in some depth what you were asking, and preferably you did too. The answer did not, of course, always come in one session ‹ even though the sessions could last for many hours, past meal times and past other appointments that you forgot about because you were so engrossed. His memory was prodigious, and when he encountered a problem he 'worried it', like a dog with a bone. He might not have all the insight he wanted when the question was first raised, or even during the next few days or weeks ‹ but he wouldn't forget. You might encounter him some years later, and he'd say: "I've been thinking about what you said, and ....".
He was at once friendly, open, uncommonly generous, and extremely bright. He was, to those who were privileged to work with him or otherwise benefit from his insights, simply without peer as a one-on-one teacher. In the 40's and '50's, many who worked with him felt complimented when he would say "How can you be so god-damned stupid?", since we realized that he expected us to understand and that, frustrated though he might be with our slowness, he would not give up until we understood, or left. In his later years, he learned patience and mellowed somewhat, and those who couldn't follow an abstruse line of reasoning he was explaining might be asked "What do I have to do, say it louder?" But never, and I do mean never, was there any animosity involved in what might seem to some to be harsh remarks. Nor did Verner's own ego ever intrude. He was selfless, far more so than almost anyone imaginable with his level of intellect and accomplishment. He was interested in getting things right, not in who got the credit, and was never afraid to admit his errors and his own limitations, although he overestimated them (as he, generously, did the abilities of some of his collaborators).
He is best known for his contributions in electron and X-ray diffraction. He thought that his most important contribution had been in the early days of electron diffraction, for development of techniques for the visual interpretation of the scattering of electrons by gas molecules. None of the structures reported from his productive group had later to be revised, when sector methods gave greater resolution and precision. But he published in many other fields as well ‹ one of his final papers (with J. Waser) was on the "Global Thermodynamics of Systems That Include Stressed Solids", and he was saddened that he could not interest any colleague in studying it intently enough to discuss it with him meaningfully. At least one of his papers became a "Citation Classic" in the Science Citation Index. However, his total publication list probably didn't reach 200 papers, because he was a perfectionist when writing a paper, and because he was so readily distracted by the intriguing problems presented by those who sought him out. His generous spirit, his penetrating intellect, his breadth of interests and curiosity, and his selflessness, led almost everyone within his orbit to use him as a consultant. There is little doubt that if there were a "Science Advisor Acknow-ledgment Index", he would have ranked at or very near the top. It has been estimated that during the 1940s and '50s, at least one third, and perhaps as many as one half, of the papers published by the "Gates and Crellin Laboratories" (the Caltech Division of Chemistry) concluded with a phrase such as "We are grateful to Professor Verner Schomaker for helpful discussions", or "The valuable insights provided by our colleague Verner Schomaker helped to make this work possible". And these papers covered the gamut of work in the Division, not just in diffraction, but in quantum mechanics, immunochemistry, nmr, spectroscopy, thermodynamics, inorganic and organic chemistry. In those years, the reference "V. Schomaker, unpublished" was so common (in others' ppers especially) that it could be recognized by the astute as what Patterson meant by "Vernished" in his famous spoof of the Acta Crystallographica telegraphic style.
A native of Nebraska, where he grew up on a farm, he earned a BS from that state's University in 1934 and an MS in 1935. He then moved to Pasadena, where Pauling quickly recognized his uncommon qualities. After receiving a PhD in 1938, he went up the academic ladder in Chemistry at Caltech (taking time out for war-time research from 1942 to 1945). He received the ACS Award in Pure Chemistry in 1949, and served as ACA President in 1961-62. In 1958 he left academic work to join the Union Carbide Research Institute (just north of New York City), where he spent 7 years ‹ but when it became apparent that the initial promise of something modelled on the Bell Labs or what was then the Shell Development Lab was never going to materialize, he joined the faculty of the Department of Chemistry at the University of Washington in Seattle, serving initially for 5 years as Chair, during an important time for faculty growth. He became Professor Emeritus in 1984. After his retirement, he was also a Faculty Assoc. at Caltech, dividing his time about equally between Pasadena and Seattle.
He is survived by his wife Judy, his sisters Helen and Mariana, his sons David, Eric, and Peter, and eight grandchildren. His family has requested that donations in his memory be made to the Verner Schomaker Memorial Fund, c/o California Institute of Technology, Office of Donor Relations, Mail Code 105-40, Pasadena, CA 91125. The fund will be used to support student research.
The complete text of this 21-line paper by "A. L. Pon" is reproduced in Patterson and Pattersons, edited by Jenny Glusker, Betty Patterson, and Miriam Rossi, Oxford University Press (1987), p. 618
Kenneth Trueblood

CALENDAR OF MEETINGS
To conserve space and paper, contact points for most meetings announced in previous newsletter issues will not be repeated. More complete information can be found in back issues of the newsletter.
JULY 1997
20 - 25 ACA '97 St. Louis, MO. Contact: Lee Brammer FAX: (314) 553-5342 E-mail: Lee.Brammer@ umsl.edu.
27 - 1 Sagamore XII. Charge, Spin and Momentum Densities, Waskeslu, Canada. Contact Bev Robertson, Dept. of Physics, U. of Regina, Saskatchewan, Canada S4S 0A2. e-mail: robertsb@leroy.cc. uregina.ca.
AUGUST 1997
4 - 8 46th Annual Denver X-ray Conference, Steamboat Springs, CO. In addition to XRD and XRF Sessions and Workshops, Program will include a symposium on High Resolution Diffraction and X-Ray Topography. Contact: Carole Collier phone (303) 871-3515, FAX: (303) 871-4450, e-mail: denxrcon@du. edu, The program may be found on the University of Denver - Engineering Department home page: http://www.engr.du.edu
31 - 4 XVII Conference on Applied Crystallography, Katowice, Poland. Contact: Dr. Danuta Stroz, Institute of Physics and Chemistry of Materials, University of Silesia, ul. Bankowa 12, 40-007 Katowice, Poland. FAX: 48-32-596929, e-mail usctoux1.cto. us.edu.pl
3-8 Structural Chemistry Indaba II - Intermolecular Interactions. Kruger National Park, South Africa. Contact: Lesley Stephenson, Structural Chemistry Indaba, CEE Conference Office, PO Box 327, Wits University, WITS 2050, South Africa. tel. +27-11-716-5091, FAX: +27-11-716-7835. Conference WWW page: http://www.gh. wits.ac.za/indaba. Any emails should be directed to "indaba-org@ hobbes.gh.wits.ac.za".

4 - 14 Sixth Annual ACA Summer Course for Crystallographers. University of Georgia, Athens, GA. Contact: Prof. Bi-Cheng Wang, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602. tel. (706) 542-1747; FAX: (706) 542-3077.
17 - 21 International Conference on Neutron Scattering. Toronto, Canada. Contact: P. H. Green, Solid State Division, Oak Ridge National Laboratory, P. O. Box 2008, Oak Ridge, TN 37831-6033, tel. (423)576-1864, FAX: (423) 574-4143, e-mail phg@ornl.gov. WWW site: http://www.physics.utoronto. ca/icns/icns.html.
SEPTEMBER 1997
8 - 18 Fifth Oxford Summer School on Neutron Scattering, Oxford, England. Contact Dr. C. J. Carlile, ISIS Pulsed Source, Rutherford Appleton Laboratory, Chilton, Didcot, Oxon OX11 0QX, England. e-mail: cjc@isis.rl.ac.uk.
20 - 23 III Iberoamerican Congress of Biophysics, Buenos Aires, Argentina. Contact Dr. G. L. Alonso, Catedra de Biofisica, Facultad de Odontologia, M T de Alvear 2142, 1122 Buenos Aires, Argentina. e-mail: rtjpaul@criba. edu.ar.
25 - 28 Fifth Workshop on Powder Diffraction - Ab Initio Structure Determination of Molecular Solids from Powder Diffraction. Laboratory of Crystallography, University of Bayreuth, Germany. Updated information is available at: http://www.uni-bayreuth.de/departments/crystal/teaching/workshop. E-mail: robert. dinnebier@uni-bayreuth.de.
28 - Oct. 1 Eastern Regional Conference on Crystal Growth & Epitaxy - ACCGE/east-97. Bally's Park Place Hotel & Casino, Atlantic City, N.J. Contact: Rose Scripa, Univ. of Alabama at Birmingham, Dept. of Materials Engineering, 1150 10th Avenue S, Birmingham AL 35294-4461. tel. 205-934-8453, fax 205-934-8485, email rscipa@eng. uab.edu.

OCTOBER 1997
26-29 1997 International Conference on Image Processing, Santa Barbara, CA. Contact: Prof. B. S. Manjunath, University of California, Santa Barbara, CA e-mail manj@ece.ucsb.edu, Web site: http://vivaldi.ece.ucsb.edu/ICIP97/icip97.html
JULY 1998
13 - 17 IUPAC Macro 98: 37th International Symposium on Macromolecules. Contact: Macro 98 Australia, Chem. Department, The University of Queensland, Brisbane, Queensland 4072, Australia.
19-24 ACA'98 Washington, D.C. Program Chair: Louis Delbaere (univ. of Saskatchewan). Local Co-chairs: Terrell Vanderah (NIST) and Vicky Karen (NIST).
AUGUST 1998
10-14 IMA'98 17th General Meeting, Int. Mineralogical Assoc., Toronto, Canada. The meeting will be centered on extensive scientific sessions, preceded and succeeded by field trips across Canada and the US including important mineral locations, ore deposits, sites of impact craters, and classic petrologic localities. Contact: Dr. Eva Schandl, Department of Geology, University of Toronto, Earth Sciences Centre, 22 Russell St., Toronto, CA M5S 3B1, e-mail ima98@quartz.geolog. utoronto.ca, Web site: http://www:geology. utoronto.can/IMA98
22-25 6th European Powder Diffraction Conference (EPDIC-6). Budapest, Hungary. Contact: Prof. Tamas Ungar (chairman), Dept. of General Physics, Eotvos University, H-1445 Budapest, POB 323, Muzeum krt 6-8, tel./fax (36-1) 2669833, e-mail: ungar@ludens.elte.hu
May 1999
ACA'99. Buffalo, NY. Local Chair: David Smith (HWI), Program Chair: Steve Ealick (Cornell).
AUGUST 1999
4 - 13 18th IUCr General Assembly and Intl. Congress of Crystallography. Glasgow, Scotland. Contact:C. J. Gilmore, Dept. of Chem, U. of Glasgow, Glasgow G128QQ, Scotland. FAX: 41-330-4418, e-mail iucr99@chem.gla.ac.uk

POSITIONS AVAILABLE
It is expected that the employers listed in this publication are equal opportunity employers who wish to receive applications from qualified persons regardless of age, national origin, race, religion, sex or physical handicaps. Please inform the Editor when the positions are filled, and of any positions that do not give opportunities to all applicants. Ads will appear in two successive newsleters unless the Editor is notified that the advertisement should be continued longer or discontinued earlier.
Research Biochemist
Pharmacia & Upjohn, Inc. is the world's ninth largest pharmaceutical company. We are involved in areas such as Oncology and Infectious, Inflammatory, Central Nervous System, and Metabolic Diseases to help people live longer and fuller lives. At Pharmacia & Upjohn you can make a difference, not only for the sake of your career, but also for the millions of people around the world whose lives will be enhanced by the solutions you help us provide.
The successful applicant will work as a member of the macromolecular crystallography laboratory. Primary responsibilities include the preparation of biological macromolecules and drug complexes for crystallization experiments. The work requires the ability to set up and analyze a variety of macromolecular crystallization experiments, to collect single crystal data and to process the data for structural determination, with minimal supervision. This position also requires the direct interaction with crystallographers as well as other personnel in structural and analytical chemistry. The successful candidate will be expected to work with the supervisory scientist to expand the existing repertoire of crystallization methodology and to assist in the development of alternative crystallization strategies for specific macromolecule targets and to communicate the results of crystallization efforts and structural biology results to other researchers. Experience in protein purification, enzymology, molecular biology or biophysics is desirable.
The successful candidate will have a M.S. in Biochemistry, or B.S. with minimum of two (2) to three (3) years directly related laboratory experience or equivalent; experience with crystallization of macromolecules is required.
Pharmacia & Upjohn offers a stimulating, multi-disciplinary research environment in modern facilities at our Pharma Product Center in Kalamazoo. Our region offers an outstanding mix of cultural and recreational pursuits and an attractive cost of living. Excellent salary and benefit packages are provided.
For confidential consideration, please send your resume and a description of your research experience to: Pharmacia & Upjohn, Recruiting, Ad #970179, 7000 Portage Road, Kalamazoo, MI 49001. If you are responding by e-mail, include your resume as part of the message (not as an attachment) to: recruit@am.pnu.com.
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POSTDOCTORAL POSITIONS

Biophysics, Biochemistry and Biomathematics.: Two NSF-funded fellowships are available immediately for interdisciplinary studies