English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Preprint

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

MPS-Authors
/persons/resource/persons202768

Schulz,  E.-C.
University Medical Center Hamburg-Eppendorf (UKE);
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Institute for Nanostructure and Solid State Physics, University of Hamburg;

/persons/resource/persons241300

Leimkohl,  J.-P.
Machine Physics, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

/persons/resource/persons241303

Schikora,  H.
Machine Physics, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

/persons/resource/persons182596

Tellkamp,  F.
Machine Physics, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

/persons/resource/persons209117

Mehrabi,  P.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Institute for Nanostructure and Solid State Physics, University of Hamburg;

External Resource
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
Supplementary Material (public)
There is no public supplementary material available
Citation

Schulz, E.-C., Prester, A., von Stetten, D., Gore, G., Hatton, C. E., Bartels, K., et al. (2024). Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography. doi:10.1101/2021.11.07.467596.


Cite as: https://hdl.handle.net/21.11116/0000-000F-FB2B-7
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.