IUCr journals

Structure-factor analysis of femtosecond microdiffraction patterns from protein nanocrystals

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

[Microdiffraction] 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.

R. A. Kirian, T. A. White, J. M. Holton, H. N. Chapman, P. Fromme, A. Barty, L. Lomb, A. Aquila, F. R. N. C. Maia, A. V. Martin, R. Fromme, X. Wang, M. S. Hunter, K. E. Schmidt and J. C. H. Spence

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