Journal
IUCRJ
Volume 8, Issue -, Pages 784-792Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2052252521007053
Keywords
time-resolved crystallography; enzymology; protein structure; structure determination; X-ray crystallography; enzyme mechanisms; millisecond mix-and-quench crystallography; protein dynamics; structural biology
Funding
- National Institutes of Health, National Institute of General Medical Sciences [R01-GM127528]
- National Science Foundation, Directorate for Biological Sciences [MCB-1330685]
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Millisecond mix-and-quench crystallography (MMQX) has been developed to achieve millisecond time-resolved data using fewer crystals and routine remote synchrotron data collection. This approach lowers the barrier to time-resolved crystallography and enables a broad expansion in structural studies of protein dynamics.
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.
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