Structure-factor analysis of femtosecond microdiffraction patterns from protein nanocrystals

Acta Cryst. (2011). A67, 131–140 (doi.org/10.1107/S0108767310050981)

Simulated femtosecond microdiffraction pattern from membrane protein nanocrystal, showing 'shape-transform' fringes running between Bragg partial reflections. These are expected to provide new solutions to the phase problem [Optics Express (2011). 19, 2866].

The invention of the pulsed hard X-ray laser is providing new opportunities for structural biology. Here Kirian and co-workers describe their 'Monte Carlo' data analysis method, developed for merging millions of 'partial' femtosecond snap-shot diffraction patterns from individual protein nanocrystals, running in a fine liquid jet in random orientations across the Linac Coherent Light Source at SLAC. This 'diffract-before-destroy' method is expected to be powerful for time-resolved crystallography, for proteins which don’t grow large crystals, and as a means to minimize radiation damage. Experimental results for this work (and for LCLS diffraction and imaging of a single virus) were published recently in Nature by Chapman et al. and by Siebert et al.

See related article on Workshop on X-ray Lasers for Biology.