W0081

Protein Crystallography with Spallation Neutrons. Paul Langan, Xinmin Li and Benno P. Schoenborn, Bioscience Div., Los Alamos National Laboratory, Los Alamos NM 87544, USA.

Spallation neutrons offer a new arena for protein crystallography in the emerging era of Proteomics. Neutron protein crystallography has the potential to play an important auxiliary role in Proteomics by providing unique information on the catalytic mechanism of newly discovered enzymes. This potential derives from the fact that neutron diffraction is a powerful technique for locating functionally important hydrogen atoms and water molecules. Los Alamos National Laboratory’s Bioscience Division runs a Protein Crystallography (PCS) station at Los Alamos Neutron Science Center’s neutron spallation source as a user facility for the structural biology community. This station, funded by the Department of Energy Office of Biological and Environmental Research, is the only resource of its kind in North America, the first to be built at a spallation source, and the first to use time-of-flight (TOF) techniques. At spallation sources neutrons are produced in “time-stamped” pulses. By recording TOF information, the corresponding wavelength of each detected neutron can be calculated. TOF techniques in combination with large electronic position sensitive detectors allow wavelength-resolved Laue patterns to be collected. An overview of the user facility will be given and some recent results presented.