Reproducible radiation-damage processes in proteins irradiated by intense x-ray pulses

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
Stefan P Hau-Riege, Brian J Bennion

Abstract

X-ray free-electron lasers have enabled femtosecond protein nanocrystallography, a novel method to determine the structure of proteins. It allows time-resolved imaging of nanocrystals that are too small for conventional crystallography. The short pulse duration helps in overcoming the detrimental effects of radiation damage because x rays are scattered before the sample has been significantly altered. It has been suggested that, fortuitously, the diffraction process self-terminates abruptly once radiation damage destroys the crystalline order. Our calculations show that high-intensity x-ray pulses indeed trigger a cascade of damage processes in ferredoxin crystals, a particular metalloprotein of interest. However, we found that the damage process is initially not completely random. Correlations exist among the protein monomers, so that Bragg diffraction still occurs in the damaged crystals, despite significant atomic displacements. Our results show that the damage process is reproducible to a certain degree, which is potentially beneficial for the orientation step in single-molecule imaging.

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Citations

Mar 2, 2019·Acta Crystallographica. Section D, Structural Biology·Karol Nass
Oct 3, 2019·The Journal of Chemical Physics·Kaoru YamazakiHirohiko Kono
Jan 3, 2019·Annual Review of Biochemistry·Henry N Chapman
Apr 15, 2020·Nature Communications·Karol NassIlme Schlichting
Sep 7, 2017·IUCrJ·J C H Spence

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