TY  - JOUR
AU  - Schulz, Eike
AU  - Prester, Andreas
AU  - Stetten, David von
AU  - Gore, Gargi
AU  - Hatton, Caitlin
AU  - Bartels, Kim
AU  - Leimkohl, Jan-Philipp
AU  - Schikora, Hendrik
AU  - Ginn, Helen
AU  - Tellkamp, Friedjof
AU  - Mehrabi, Pedram
TI  - Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography
JO  - Nature Communications
VL  - 16
IS  - 1
SN  - 2041-1723
CY  - [London]
PB  - Springer Nature
M1  - PUBDB-2025-02618
SP  - 6553
PY  - 2025
AB  - The vast majority of protein structures are determined at cryogenic temperatures, which are far from physiological conditions. Nevertheless, it is well established that temperature is an essential thermodynamic parameter for understanding the conformational dynamics and functionality of proteins in their native environments. Time-resolved crystallography is a technique that aims to elucidate protein function by examining structural alterations during processes such as ligand binding, catalysis, or allostery. However, this approach is typically conducted under ambient conditions, which may obscure crucial conformational states, that are only visible at physiological temperatures. In this study, we directly address the interplay between protein structure and activity via a method that enables multi-temperature, time-resolved serial crystallography experiments in a temperature window from below 10 °C to above 70 °C. Via this 5D-SSX, time-resolved experiments can now be carried out at physiological temperatures and with long time delays, providing insights into protein function and enzyme catalysis. Our findings demonstrate the temperature-dependent modulation of turnover kinetics for the mesophilic β-lactamase CTX-M-14 and the thermophilic enzyme xylose isomerase, within the full protein structure.
LB  - PUB:(DE-HGF)16
DO  - DOI:10.1038/s41467-025-61631-2
UR  - https://bib-pubdb1.desy.de/record/634794
ER  -