4ET8 : Hen egg-white lysozyme solved from 40 fs free-electron laser pulse data

  • R. Bruce Doak (Contributor)
  • Thomas R M Barends (Contributor)
  • Robert L. Shoeman (Contributor)
  • Ilme Schlichting (Contributor)
  • Petra Fromme (Contributor)
  • Mark S. Hunter (Contributor)
  • Christopher Kupitz (Contributor)
  • Marc Messerschmidt (Contributor)
  • Lars Redecke (Contributor)
  • M. Marvin Seibert (Contributor)
  • Thomas A. White (Contributor)
  • Nadia Zatsepin (Contributor)
  • Henry N. Chapman (Contributor)
  • Anton Barty (Contributor)
  • Donald Schafer (Contributor)
  • Michael J. Bogan (Contributor)
  • Garth J. Williams (Contributor)
  • S├ębastien Boutet (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Release Date:2012-06-13
Deposition Date:2012-04-24
Revision Date:2012-08-08#2015-11-18#2017-11-15#2018-02-14
Molecular Weight:14389.6
Macromolecule Type:Protein
Residue Count:129
Atom Site Count:1003

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.
Date made available2012

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