Complementarity of neutron, XFEL and synchrotron crystallography for defining the structures of metalloenzymes at room temperature

Complementarity of neutron, XFEL and synchrotron crystallography for defining the structures of metalloenzymes at room temperature

Room-temperature macromolecular crystallography allows protein structures to be determined under close-to-physiological conditions, permits dynamic freedom in protein motions and enables time-resolved studies. In the case of metalloenzymes that are highly sensitive to radiation damage, such room-tem...

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Bibliographic Details
Main Authors: Tadeo Moreno-Chicano, Leiah M. Carey, Danny Axford, John H. Beale, R. Bruce Doak, Helen M. E. Duyvesteyn, Ali Ebrahim, Robert W. Henning, Diana C. F. Monteiro, Dean A. Myles, Shigeki Owada, Darren A. Sherrell, Megan L. Straw, Vukica Šrajer, Hiroshi Sugimoto, Kensuke Tono, Takehiko Tosha, Ivo Tews, Martin Trebbin, Richard W. Strange, Kevin L. Weiss, Jonathan A. R. Worrall, Flora Meilleur, Robin L. Owen, Reza A. Ghiladi, Michael A. Hough
Format: Article
Language:English
Published: International Union of Crystallography 2022-09-01
Series:IUCrJ
Subjects:
serial femtosecond crystallography
serial synchrotron crystallography
neutron crystallography
xfels
room temperature
metalloenzymes
Online Access:http://scripts.iucr.org/cgi-bin/paper?S2052252522006418

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http://scripts.iucr.org/cgi-bin/paper?S2052252522006418

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