A Bright Future for Serial Femtosecond Crystallography with XFELs

Trends Biochem Sci. 2017 Sep;42(9):749-762. doi: 10.1016/j.tibs.2017.06.007. Epub 2017 Jul 18.

Abstract

X-ray free electron lasers (XFELs) have the potential to revolutionize macromolecular structural biology due to the unique combination of spatial coherence, extreme peak brilliance, and short duration of X-ray pulses. A recently emerged serial femtosecond (fs) crystallography (SFX) approach using XFEL radiation overcomes some of the biggest hurdles of traditional crystallography related to radiation damage through the diffraction-before-destruction principle. Intense fs XFEL pulses enable high-resolution room-temperature structure determination of difficult-to-crystallize biological macromolecules, while simultaneously opening a new era of time-resolved structural studies. Here, we review the latest developments in instrumentation, sample delivery, data analysis, crystallization methods, and applications of SFX to important biological questions, and conclude with brief insights into the bright future of structural biology using XFELs.

Keywords: X-ray free electron laser; lipidic cubic phase; membrane proteins; molecular movies; protein complexes; structural biology.

Publication types

  • Review
  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography / methods*
  • Electrons*
  • Lasers*
  • Macromolecular Substances / chemistry
  • Time Factors
  • X-Rays

Substances

  • Macromolecular Substances