Millisecond mix-and-quench crystallography (MMQX) enables time-resolved studies of PEPCK with remote data collection

Time-resolved crystallography of biomolecules in action has advanced rapidly as methods for serial crystallography have improved, but the large number of crystals and the complex experimental infrastructure that are required remain serious obstacles to its widespread application. Here, millisecond m...

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Bibliographic Details
Published in:IUCrJ 2021-09, Vol.8 (Pt 5), p.784-792
Main Authors: Clinger, Jonathan A, Moreau, David W, McLeod, Matthew J, Holyoak, Todd, Thorne, Robert E
Format: Article
Language:English
Subjects:
Biomolecules
Crystallography
Data collection
Data entry
Dynamic structural analysis
enzyme mechanisms
enzymology
millisecond mix-and-quench crystallography
Phosphates
protein dynamics
protein structure
Research Papers
structural biology
structure determination
Synchrotrons
time-resolved crystallography
x-ray crystallography
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Summary:Time-resolved crystallography of biomolecules in action has advanced rapidly as methods for serial crystallography have improved, but the large number of crystals and the complex experimental infrastructure that are required remain serious obstacles to its widespread application. Here, millisecond mix-and-quench crystallography (MMQX) has been developed, which yields millisecond time-resolved data using far fewer crystals and routine remote synchrotron data collection. To demonstrate the capabilities of MMQX, the conversion of oxaloacetic acid to phosphoenolpyruvate by phosphoenolpyruvate carboxy-kinase (PEPCK) is observed with a time resolution of 40 ms. By lowering the entry barrier to time-resolved crystallography, MMQX should enable a broad expansion in structural studies of protein dynamics.
ISSN:2052-2525
2052-2525
DOI:10.1107/S2052252521007053