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000634794 1001_ $$0P:(DE-H253)PIP1019225$$aSchulz, Eike$$b0$$eCorresponding author
000634794 245__ $$aProbing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography
000634794 260__ $$a[London]$$bSpringer Nature$$c2025
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000634794 520__ $$aThe vast majority of protein structures are determined at cryogenic temperatures, which are far from physiological conditions. Nevertheless, it is well established that temperature is an essential thermodynamic parameter for understanding the conformational dynamics and functionality of proteins in their native environments. Time-resolved crystallography is a technique that aims to elucidate protein function by examining structural alterations during processes such as ligand binding, catalysis, or allostery. However, this approach is typically conducted under ambient conditions, which may obscure crucial conformational states, that are only visible at physiological temperatures. In this study, we directly address the interplay between protein structure and activity via a method that enables multi-temperature, time-resolved serial crystallography experiments in a temperature window from below 10 °C to above 70 °C. Via this 5D-SSX, time-resolved experiments can now be carried out at physiological temperatures and with long time delays, providing insights into protein function and enzyme catalysis. Our findings demonstrate the temperature-dependent modulation of turnover kinetics for the mesophilic β-lactamase CTX-M-14 and the thermophilic enzyme xylose isomerase, within the full protein structure.
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000634794 536__ $$0G:(GEPRIS)194651731$$aDFG project G:(GEPRIS)194651731 - EXC 1074: Hamburger Zentrum für ultraschnelle Beobachtung (CUI): Struktur, Dynamik und Kontrolle von Materie auf atomarer Skala (194651731)$$c194651731$$x2
000634794 536__ $$0G:(GEPRIS)451079909$$aDFG project G:(GEPRIS)451079909 - Untersuchung allosterischer Mechanismen durch zeitaufgelöste serielle Synchrotronkristallographie (451079909)$$c451079909$$x3
000634794 536__ $$0G:(GEPRIS)458246365$$aDFG project G:(GEPRIS)458246365 - Zeitaufgelöste Strukturanalysde der extended spectrum Beta-Lactamase CTX-M-14 (458246365)$$c458246365$$x4
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000634794 7001_ $$0P:(DE-H253)PIP1086208$$aPrester, Andreas$$b1
000634794 7001_ $$0P:(DE-H253)PIP1083129$$aStetten, David von$$b2
000634794 7001_ $$0P:(DE-H253)PIP1099521$$aGore, Gargi$$b3
000634794 7001_ $$0P:(DE-H253)PIP1080280$$aHatton, Caitlin$$b4
000634794 7001_ $$0P:(DE-H253)PIP1081587$$aBartels, Kim$$b5
000634794 7001_ $$0P:(DE-H253)PIP1080602$$aLeimkohl, Jan-Philipp$$b6
000634794 7001_ $$0P:(DE-H253)PIP1029493$$aSchikora, Hendrik$$b7
000634794 7001_ $$0P:(DE-H253)PIP1032871$$aGinn, Helen$$b8$$udesy
000634794 7001_ $$0P:(DE-H253)PIP1007800$$aTellkamp, Friedjof$$b9$$eCorresponding author
000634794 7001_ $$0P:(DE-H253)PIP1029103$$aMehrabi, Pedram$$b10$$eCorresponding author
000634794 773__ $$0PERI:(DE-600)2553671-0$$a10.1038/s41467-025-61631-2$$gVol. 16, no. 1, p. 6553$$n1$$p6553$$tNature Communications$$v16$$x2041-1723$$y2025
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