E pluribus unum, no more: from one crystal, many conformations

Curr Opin Struct Biol. 2014 Oct:28:56-62. doi: 10.1016/j.sbi.2014.07.005. Epub 2014 Aug 9.


Several distinct computational approaches have recently been implemented to represent conformational heterogeneity from X-ray crystallography datasets that are averaged in time and space. As these modeling methods mature, newly discovered alternative conformations are being used to derive functional protein mechanisms. Room temperature X-ray data collection is emerging as a key variable for sampling functionally relevant conformations also observed in solution studies. Although concerns about radiation damage are warranted with higher temperature data collection, 'diffract and destroy' strategies on X-ray free electron lasers may permit radiation damage-free data collection. X-ray crystallography need not be confined to 'static unique snapshots'; these experimental and computational advances are revealing how the many conformations populated within a single crystal are used in biological mechanisms.

Publication types

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

MeSH terms

  • Crystallography, X-Ray*
  • Models, Molecular
  • Molecular Conformation*