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Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis

An estimated half of all proteins contain a metal, with these being essential for a tremendous variety of biological functions. X-ray crystallography is the major method for obtaining structures at high resolution of these metalloproteins, but there are considerable challenges to obtain intact struc...

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Detalles Bibliográficos
Autores principales: Hough, Michael A., Owen, Robin L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8667872/
https://www.ncbi.nlm.nih.gov/pubmed/34455163
http://dx.doi.org/10.1016/j.sbi.2021.07.007
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author Hough, Michael A.
Owen, Robin L.
author_facet Hough, Michael A.
Owen, Robin L.
author_sort Hough, Michael A.
collection PubMed
description An estimated half of all proteins contain a metal, with these being essential for a tremendous variety of biological functions. X-ray crystallography is the major method for obtaining structures at high resolution of these metalloproteins, but there are considerable challenges to obtain intact structures due to the effects of radiation damage. Serial crystallography offers the prospect of determining low-dose synchrotron or effectively damage free XFEL structures at room temperature and enables time-resolved or dose-resolved approaches. Complementary spectroscopic data can validate redox and or ligand states within metalloprotein crystals. In this opinion, we discuss developments in the application of serial crystallographic approaches to metalloproteins and comment on future directions.
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spelling pubmed-86678722021-12-15 Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis Hough, Michael A. Owen, Robin L. Curr Opin Struct Biol Article An estimated half of all proteins contain a metal, with these being essential for a tremendous variety of biological functions. X-ray crystallography is the major method for obtaining structures at high resolution of these metalloproteins, but there are considerable challenges to obtain intact structures due to the effects of radiation damage. Serial crystallography offers the prospect of determining low-dose synchrotron or effectively damage free XFEL structures at room temperature and enables time-resolved or dose-resolved approaches. Complementary spectroscopic data can validate redox and or ligand states within metalloprotein crystals. In this opinion, we discuss developments in the application of serial crystallographic approaches to metalloproteins and comment on future directions. Elsevier Science 2021-12 /pmc/articles/PMC8667872/ /pubmed/34455163 http://dx.doi.org/10.1016/j.sbi.2021.07.007 Text en © 2021 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Hough, Michael A.
Owen, Robin L.
Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis
title Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis
title_full Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis
title_fullStr Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis
title_full_unstemmed Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis
title_short Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis
title_sort serial synchrotron and xfel crystallography for studies of metalloprotein catalysis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8667872/
https://www.ncbi.nlm.nih.gov/pubmed/34455163
http://dx.doi.org/10.1016/j.sbi.2021.07.007
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