ArticleActa crystallographica. Section D, Structural biology2022
Probing ligand binding of endothiapepsin by `temperature-resolved' macromolecular crystallography.
Article in Acta crystallographica. Section D, Structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- 50th anniversary of the Stanford SSRL synchrotron radiation and protein crystallography initiative.Journal of synchrotron radiation · 2026Article
- Room-temperature X-ray fragment screening with serial crystallography.Nature communications · 2025Article
- Evolution of macromolecular crystallography beamlines at the Swiss Light Source and SwissFEL.Journal of synchrotron radiation · 2025Article
- Advancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron.Communications chemistry · 2025Article
- In situ serial crystallography facilitates 96-well plate structural analysis at low symmetry.IUCrJ · 2024Article
- A snapshot love story: what serial crystallography has done and will do for us.Acta crystallographica. Section D, Structural biology · 2024Review
- Cryo2RT: a high-throughput method for room-temperature macromolecular crystallography from cryo-cooled crystals.Acta crystallographica. Section D, Structural biology · 2024Article
- Fragment-based screening targeting an open form of the SARS-CoV-2 main protease binding pocket.Acta crystallographica. Section D, Structural biology · 2024Article
- A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers.Nature communications · 2023Article
- Micro-structured polymer fixed targets for serial crystallography at synchrotrons and XFELs.IUCrJ · 2023Article
- Article
- SDU - software for high-throughput automated data collection at the Swiss Light Source.Journal of synchrotron radiation · 2023Article
- Introduction to the virtual thematic issue on room-temperature biological crystallography.IUCrJ · 2023Article
- Introduction to the virtual thematic issue on room-temperature biological crystallography.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Relating protein crystal structure to ligand-binding thermodynamics.Acta crystallographica. Section F, Structural biology communications · 2022Article
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14 authors.
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Abstract
Continuous developments in cryogenic X-ray crystallography have provided most of our knowledge of 3D protein structures, which has recently been further augmented by revolutionary advances in cryoEM. However, a single structural conformation identified at cryogenic temperatures may introduce a fictitious structure as a result of cryogenic cooling artefacts, limiting the overview of inherent protein physiological dynamics, which play a critical role in the biological functions of proteins. Here, a room-temperature X-ray crystallographic method using temperature as a trigger to record movie-like structural snapshots has been developed. The method has been used to show how TL00150, a 175.15 Da fragment, undergoes binding-mode changes in endothiapepsin. A surprising fragment-binding discrepancy was observed between the cryo-cooled and physiological temperature structures, and multiple binding poses and their interplay with DMSO were captured. The observations here open up new promising prospects for structure determination and interpretation at physiological temperatures with implications for structure-based drug discovery.
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