Abstract

In late 2009 the world's first hard X-ray laser facility (the LCLS) starts operation at Stanford. Our beam time will use a jet of protein nanocrystals to evaluate a new idea for structural biology-that a sufficiently short and intense pulse of X-rays will terminate before atoms move or radiation damage can begin. We will collect "snap-shot" 70 fs diffraction patterns from sub-micron Photosystem I membrane protein crystallites made in the Fromme lab at ASU. 30 patterns are read out per second, giving 20 Terrabytes of data per day. If beamtime allows, we will also collect patterns from individual viruses, and clusters of viruses. I will describe our new approach for extracting the image of one particle from the scattering from many particles lying in random orientations. Finally, the protein-beam injector designed by Bruce Doak for the LCLS, and developed here in recent years by Weierstall and others, will be described.