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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Egile Nagusiak:	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
Formatua:	Artigo
Hizkuntza:	Inglês
Argitaratua:	International Union of Crystallography 2022-09-01
Saila:	IUCrJ
Gaiak:	serial femtosecond crystallography serial synchrotron crystallography neutron crystallography xfels room temperature metalloenzymes
Sarrera elektronikoa:	http://scripts.iucr.org/cgi-bin/paper?S2052252522006418
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