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

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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Bibliographic Details
Main Authors: Daniel A Keedy, Lillian R Kenner, Matthew Warkentin, Rahel A Woldeyes, Jesse B Hopkins, Michael C Thompson, Aaron S Brewster, Andrew H Van Benschoten, Elizabeth L Baxter, Monarin Uervirojnangkoorn, Scott E McPhillips, Jinhu Song, Roberto Alonso-Mori, James M Holton, William I Weis, Axel T Brunger, S Michael Soltis, Henrik Lemke, Ana Gonzalez, Nicholas K Sauter, Aina E Cohen, Henry van den Bedem, Robert E Thorne, James S Fraser
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2015-09-01
Series:eLife
Subjects:
protein dynamics
x-ray free electron laser
enzymology
Online Access:https://elifesciences.org/articles/07574

Internet

https://elifesciences.org/articles/07574

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