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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Detalles Bibliográficos
Autores principales: Moreno-Chicano, Tadeo, Carey, Leiah M., Axford, Danny, Beale, John H., Doak, R. Bruce, Duyvesteyn, Helen M. E., Ebrahim, Ali, Henning, Robert W., Monteiro, Diana C. F., Myles, Dean A., Owada, Shigeki, Sherrell, Darren A., Straw, Megan L., Šrajer, Vukica, Sugimoto, Hiroshi, Tono, Kensuke, Tosha, Takehiko, Tews, Ivo, Trebbin, Martin, Strange, Richard W., Weiss, Kevin L., Worrall, Jonathan A. R., Meilleur, Flora, Owen, Robin L., Ghiladi, Reza A., Hough, Michael A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2022
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9438502/
https://www.ncbi.nlm.nih.gov/pubmed/36071813
http://dx.doi.org/10.1107/S2052252522006418

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9438502/
https://www.ncbi.nlm.nih.gov/pubmed/36071813
http://dx.doi.org/10.1107/S2052252522006418

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