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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Bibliografische gegevens
Gepubliceerd in:eLife
Hoofdauteurs: 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
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: eLife Sciences Publications, Ltd 2015
Onderwerpen:
Biophysics and Structural Biology
Online toegang: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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