Determination of damage-free crystal structure of an X-ray-sensitive protein using an XFEL

Nat Methods. 2014 Jul;11(7):734-6. doi: 10.1038/nmeth.2962. Epub 2014 May 11.

Abstract

We report a method of femtosecond crystallography for solving radiation damage-free crystal structures of large proteins at sub-angstrom spatial resolution, using a large single crystal and the femtosecond pulses of an X-ray free-electron laser (XFEL). We demonstrated the performance of the method by determining a 1.9-Å radiation damage-free structure of bovine cytochrome c oxidase, a large (420-kDa), highly radiation-sensitive membrane protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Crystallography / methods*
  • Electron Transport Complex IV / chemistry*
  • Electron Transport Complex IV / radiation effects
  • Lasers*

Substances

  • Electron Transport Complex IV