06.01.2 Femtosecond Protein Nanocrystallography at the LCLS John Spence ASU, Tempe Az, United States First results will be reported from experiments at the world's first hard X-ray laser (the Linac Coherent Light Source) at Stanford using membrane protein nanocrystals. X-ray pulses at 2 kV of femtosecond duration were used to read out 30 diffraction patterns per second from a liquid jet of protein nanocrystals sprayed across the beam. We have evaluated the idea that a sufficiently short pulse will terminate before radiation damage begins, yet contain sufficient photons to produce a useful diffraction pattern. Details of the protein-beam injector, which must provide full hydration, will be given, and the method of data analysis discussed. This involves merging diffraction data from millions of patterns from sub-micron nanocrystals of photosystem one , of varying size and in random orientations. Many terrabytes of data were collected over several days. Plans for pump-probe experiments will also be outlined. This approach allows structure analysis of proteins which do not produce large crystals, possibly without radiation damage, directly from solution and without need for cooling. This project is a large international collaboration, involving the CAMP group from three Max Plank Institutes and ASU physics. PIs include H. Chapman, P. Fromme, I. Schlichting, B. Doak, U. Weierstall, J. Uhlich, A. Barty, L. Struder, D. Rolles, the LCLS staff and the ASG team.
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