XFEL serial crystallography reveals the room temperature structure of methyl-coenzyme M reductase

XFEL serial crystallography reveals the room temperature structure of methyl-coenzyme M reductase

Methyl-Coenzyme M Reductase (MCR) catalyzes the biosynthesis of methane in methanogenic archaea, using a catalytic Ni-centered Cofactor F430 in its active site. It also catalyzes the reverse reaction, that is, the anaerobic activation and oxidation, including the cleavage of the CH bond in methane....

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Dades bibliogràfiques
Autors principals: Ohmer, Christopher J, Dasgupta, Medhanjali, Patwardhan, Anjali, Bogacz, Isabel, Kaminsky, Corey, Doyle, Margaret D, Chen, Percival Yang-Ting, Keable, Stephen M, Makita, Hiroki, Simon, Philipp S, Massad, Ramzi, Fransson, Thomas, Chatterjee, Ruchira, Bhowmick, Asmit, Paley, Daniel W, Moriarty, Nigel W, Brewster, Aaron S, Gee, Leland B, Alonso-Mori, Roberto, Moss, Frank, Fuller, Franklin D, Batyuk, Alexander, Sauter, Nicholas K, Bergmann, Uwe, Drennan, Catherine L, Yachandra, Vittal K, Yano, Junko, Kern, Jan F, Ragsdale, Stephen W
Altres autors: Massachusetts Institute of Technology. Department of Biology
Format: Article
Idioma:English
Publicat: Elsevier BV 2022
Accés en línia:https://hdl.handle.net/1721.1/146795

Internet

https://hdl.handle.net/1721.1/146795

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