ArticleNature communications2025
Probing the modulation of enzyme kinetics by multi-temperature, time-resolved serial crystallography.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Room-temperature crystal structure of a metal-dependent W-formate dehydrogenase by serial synchrotron crystallography.Acta crystallographica. Section D, Structural biology · 2026Article
- Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes.Nature chemistry · 2026Article
- Drop-on-fixed-target reaction initiation approach for serial and time-resolved crystallography.IUCrJ · 2026Article
- Temperature-Dependent Conformational Dynamics of Substrate Entrance Loops in β-Glucosidase: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2026Article
- Statistical crystallography reveals an allosteric network in SARS-CoV-2 MCommunications biology · 2026Article
- Increasing X-ray energy improves data quality in serial crystallography.Journal of synchrotron radiation · 2026Article
- Decision-making in serial crystallography: a simple test to quickly determine whether sufficient data have been collected.Acta crystallographica. Section D, Structural biology · 2026Article
- Towards patient-relevant structures: reviewing body-temperature biological macromolecules and their ligands for pharmaceutical applications.Acta crystallographica. Section D, Structural biology · 2026Review
- Binding mode of Isoxazolyl Penicillins to a Class-A β-lactamase at ambient conditions.Communications chemistry · 2025Article
- Spitrobot-2 advances time-resolved cryo-trapping crystallography to under 25 ms.Communications chemistry · 2025Article
- Exploring the dynamics of allostery through multi-dimensional crystallography.Biophysical reviews · 2024Review
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Authors and funding
11 authors.
Funding
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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