Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography
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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 mesophilic β -lactamase CTX-M-14 and for the hyperthermophilic enzyme xylose isomerase.
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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 major effect on the estimated occupancies.
Competing interests
The author declares that they have no competing interests.
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