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Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis

DOI: 10.1016/j.sbi.2021.07.007 DOI Help

Authors: Michael A. Hough (University of Essex) , Robin L. Owen (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Current Opinion In Structural Biology , VOL 71 , PAGES 232 - 238

State: Published (Approved)
Published: December 2021

Open Access Open Access

Abstract: 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.

Subject Areas: Biology and Bio-materials, Chemistry, Technique Development


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Documents:
1-s2.0-S0959440X21001093-main.pdf

Discipline Tags:

Biochemistry Catalysis Technique Development - Life Sciences & Biotech Chemistry Structural biology Life Sciences & Biotech

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