Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography
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Abstract
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
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Spitrobot-2 advances time-resolved cryo-trapping crystallography to under 25 ms
Spiliopoulou, M., Hatton, C. E., Kollewe, M., Leimkohl, J.-P., Schikora, H., Tellkamp, F., Mehrabi, P., & Schulz, E. C. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01784-9 · Cited by 2 · see citing works
Self-citationBrink, A., Helliwell, J. R., & Jacobs, F. J. F. (2025) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798325010617 · Cited by 2 · see citing works
Drop-on-fixed-target reaction initiation approach for serial and time-resolved crystallography
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X-ray free electron lasers (XFELs) in time-resolved X-ray diffraction and spectroscopy
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- Authors
- Schulz, E. C., Prester, A., von Stetten, D., Gore, G., Hatton, C. E., Bartels, K., Leimkohl, J.-P., Schikora, H., Ginn, H. M., Tellkamp, F., & Mehrabi, P.
- Affiliations
- Universität Hamburg (DE)
- University Medical Center Hamburg-Eppendorf (DE)
- Max Planck Institute for the Structure and Dynamics of Matter (DE)
- Deutsches Elektronen-Synchrotron DESY (DE)
- Corresponding author
- Schulz, Eike C.
- Tellkamp, Friedjof
- Mehrabi, Pedram
- ORCID
- Venue
- Nature Communications
- Published
- 2025-07-16
- Volume
- 16
- Issue
- 1
- Pages
- 6553-6553
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC12267849
- OpenAlex
- W4412475647
- Cited by
- 15
- References
- 84
- Citations by year
- 2026: 11 · 2025: 4
- FWCI
- 3.16
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DESY Publication Database (PUBDB) (Deutsches Elektronen-Synchrotron) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Joachim Herz Stiftung
- European Commission
- Deutsche Forschungsgemeinschaft (EXC-1074, 458246365, 451079909, 194651731)
- Bundesministerium für Bildung und Forschung (05K22GU6, 05K16GU1, 01KI2114, 05K19GU1)
- Max-Planck-Gesellschaft
- Hamburg Centre for Ultrafast Imaging (ID 194651731, EXC1074, 194651731)
- Deutsches Elektronen-Synchrotron
- HORIZON EUROPE European Research Council (101071843)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Physics and Astronomy › Radiation › Advanced X-ray Imaging Techniques
- Keywords
- time-resolved serial crystallography, enzyme kinetics, temperature dependence, CTX-M-14, beta-lactamase, xylose isomerase, thermophilic enzymes, protein conformational dynamics, protein structure-function relationship
- MeSH terms
- beta-Lactamases, Kinetics, Models, Molecular, Protein Conformation, Temperature, Thermodynamics, Crystallography, X-Ray, Aldose-Ketose Isomerases
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