PREreviews of “Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography”

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Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography

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: November 7, 2021
Server: bioRxiv
DOI: 10.1101/2021.11.07.467596

Abstract

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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PREreview by James Fraser

Authored by James Fraser

This is an excellent experimental setup and I read the manuscript with great interest. My major question has to do with the modeling in Figure 2. Is there no solvent in any of the substrate/product states or an apo state that needs to be modeled in the active site. This seems like it might have a…

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PREreviews of Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography

1 PREreview