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

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

Author information

1
Chemistry and Chemical Biology Graduate Program, University of California, San Francisco, San Francisco, CA 94158, United States.
2
Center for Systems and Synthetic Biology, University of California, San Francisco, San Francisco, CA 94158, United States.
3
Department of Bioengineering and Therapeutic Sciences and California Institute for Quantitative Biosciences, University of California, San Francisco, San Francisco, CA 94158, United States. Electronic address: james.fraser@ucsf.edu.

Abstract

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.

PMID:
25113271
PMCID:
PMC4253534
DOI:
10.1016/j.sbi.2014.07.005
[Indexed for MEDLINE]
Free PMC Article

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