Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography
E. C. Schulz, A. Prester, D. von Stetten, G. Gore, C. E. Hatton, K. Bartels, J.-P. Leimkohl, H. Schikora, H. M. Ginn, F. Tellkamp, P. Mehrabi
Abstract
We present an environmental enclosure for fixed-target serial crystallography, enabling X-ray diffraction experiments in a temperature window from below 10 {degrees}C to above 70 {degrees}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 {beta}-lactamase CTX-M-14 and for the hyperthermophilic enzyme xylose isomerase.
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