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Updated: Oct 22, 2025
Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography
Published on: April 24, 2018
Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis
Michael A Hough1, Robin L Owen2
1School of Life Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, UK.
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.
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