W0008

Protein/Membrane/Fibre Crystallography with Spallation Neutrons. Benno P. Schoenborn, Life Sciences Division, Los Alamos National Laboratory, Los Alamos, NM 87545

Suitable instruments on spallation neutron sources are ideal for diffraction studies of proteins and oriented molecular complexes. With spallation neutrons and their time dependent wavelength structure, diffraction data may be readily selected electronically with an optimal wavelength bandwidth and cover the whole Laue spectrum as time (wavelength) resolved spectra. This optimizes data quality with best peak-to-background ratios and provides adequate spatial and energy resolution to eliminate diffraction peak overlaps. To maximize flux within this energy range a partially decoupled moderator concept will be discussed using calculated flux profiles, and the impact on calculated diffraction data assessed. The design of such a structural biology neutron station at the LANSCE Spallation source will be presented. This station utilizes a focusing toroidal mirror and a large cylindrical position sensitive detector.