Mapping the conformational landscape of a dynamic enzyme by multitemperature and XFEL crystallography

Determining the interconverting conformations of dynamic proteins in atomic detail is a major challenge for structural biology. Conformational heterogeneity in the active site of the dynamic enzyme cyclophilin A (CypA) has been previously linked to its catalytic function, but the extent to which the...

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Pubblicato in:eLife
Autori principali: Keedy, Daniel A, Kenner, Lillian R, Warkentin, Matthew, Woldeyes, Rahel A, Hopkins, Jesse B, Thompson, Michael C, Brewster, Aaron S, Van Benschoten, Andrew H, Baxter, Elizabeth L, Uervirojnangkoorn, Monarin, McPhillips, Scott E, Song, Jinhu, Alonso-Mori, Roberto, Holton, James M, Weis, William I, Brunger, Axel T, Soltis, S Michael, Lemke, Henrik, Gonzalez, Ana, Sauter, Nicholas K, Cohen, Aina E, van den Bedem, Henry, Thorne, Robert E, Fraser, James S
Natura: Artigo
Lingua:Inglês
Pubblicazione: eLife Sciences Publications, Ltd 2015
Soggetti:
Biophysics and Structural Biology
Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC4721965/
https://ncbi.nlm.nih.gov/pubmed/26422513
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7554/eLife.07574
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