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

Stefan P. Hau-Riege, Brian J. Bennion

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


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.

Original languageEnglish (US)
Article number022705
JournalPhysical Review E - Statistical, Nonlinear, and Soft Matter Physics
Issue number2
StatePublished - Feb 9 2015
Externally publishedYes

ASJC Scopus subject areas

  • Condensed Matter Physics
  • Statistical and Nonlinear Physics
  • Statistics and Probability


Dive into the research topics of 'Reproducible radiation-damage processes in proteins irradiated by intense x-ray pulses'. Together they form a unique fingerprint.

Cite this