Serial femtosecond crystallography: A revolution in structural biology

Jose M. Martin-Garcia, Chelsie E. Conrad, Jesse Coe, Shatabdi Roy-Chowdhury, Petra Fromme

Research output: Contribution to journalArticle

48 Scopus citations

Abstract

Macromolecular crystallography at synchrotron sources has proven to be the most influential method within structural biology, producing thousands of structures since its inception. While its utility has been instrumental in progressing our knowledge of structures of molecules, it suffers from limitations such as the need for large, well-diffracting crystals, and radiation damage that can hamper native structural determination. The recent advent of X-ray free electron lasers (XFELs) and their implementation in the emerging field of serial femtosecond crystallography (SFX) has given rise to a remarkable expansion upon existing crystallographic constraints, allowing structural biologists access to previously restricted scientific territory. SFX relies on exceptionally brilliant, micro-focused X-ray pulses, which are femtoseconds in duration, to probe nano/micrometer sized crystals in a serial fashion. This results in data sets comprised of individual snapshots, each capturing Bragg diffraction of single crystals in random orientations prior to their subsequent destruction. Thus structural elucidation while avoiding radiation damage, even at room temperature, can now be achieved. This emerging field has cultivated new methods for nanocrystallogenesis, sample delivery, and data processing. Opportunities and challenges within SFX are reviewed herein.

Original languageEnglish (US)
Pages (from-to)32-47
Number of pages16
JournalArchives of Biochemistry and Biophysics
Volume602
DOIs
StatePublished - Jul 15 2016

    Fingerprint

Keywords

  • Membrane proteins
  • Nanocrystals
  • Protein crystallography
  • Serial femtosecond crystallography
  • X-ray free electron lasers

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this