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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Dades bibliogràfiques
Publicat a:eLife
Autors principals: 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
Format: Artigo
Idioma:Inglês
Publicat: eLife Sciences Publications, Ltd 2015
Matèries:
Biophysics and Structural Biology
Accés en línia: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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