High-resolution protein structure determination by serial femtosecond crystallography

Science. 2012 Jul 20;337(6092):362-4. doi: 10.1126/science.1217737. Epub 2012 May 31.


Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.

Publication types

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

MeSH terms

  • Animals
  • Crystallography, X-Ray / methods*
  • Lasers
  • Muramidase / chemistry
  • Muramidase / radiation effects
  • Protein Conformation*


  • hen egg lysozyme
  • Muramidase

Associated data

  • PDB/4ET8
  • PDB/4ET9
  • PDB/4ETA
  • PDB/4ETB
  • PDB/4ETC
  • PDB/4ETD
  • PDB/4ETE