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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Foilsithe in:eLife
Main Authors: 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
Formáid: Artigo
Teanga:Inglês
Foilsithe: eLife Sciences Publications, Ltd 2015
Ábhair:
Biophysics and Structural Biology
Rochtain Ar Líne: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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