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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Detalles Bibliográficos
Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2015
Materias:
Biophysics and Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721965/
https://www.ncbi.nlm.nih.gov/pubmed/26422513
http://dx.doi.org/10.7554/eLife.07574

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721965/
https://www.ncbi.nlm.nih.gov/pubmed/26422513
http://dx.doi.org/10.7554/eLife.07574

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