Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography
Authored by
Eike C. Schulz, Andreas Prester, David von Stetten, Gargi Gore, Caitlin E. Hatton, Kim Bartels, Jan-Philipp Leimkohl, Hendrik Schikora, Helen M. Ginn, Friedjof Tellkamp, and Pedram Mehrabi
Posted
Server
bioRxiv
DOI
10.1101/2021.11.07.467596
We present an environmental enclosure for fixed-target serial crystallography, enabling X-ray diffraction experiments in a temperature window from below 10 °C to above 70 °C - a universal parameter of protein function. Via 5D-SSX time-resolved experiments can now be carried out at physiological temperatures, providing fundamentally new insights into protein function. We show temperature-dependent modulation of turnover kinetics for the mesophilicβ-lactamase CTX-M-14 and for the hyperthermophilic enzyme xylose isomerase.
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