ArticleJournal of synchrotron radiation2017
Conformational variation of proteins at room temperature is not dominated by radiation damage.
Article in Journal of synchrotron radiation, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 61 citations in OpenAlex.
- Sensitive detection of structural dynamics using a statistical framework for comparative crystallography.Science advances · 2025Article
- In situ serial crystallography facilitates 96-well plate structural analysis at low symmetry.IUCrJ · 2024Article
- Identifying and avoiding radiation damage in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2024Article
- Changes in an enzyme ensemble during catalysis observed by high-resolution XFEL crystallography.Science advances · 2024Article
- From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons.Acta crystallographica. Section D, Structural biology · 2024Article
- Alternate conformations found in protein structures implies biological functions: A case study using cyclophilin A.Current research in structural biology · 2024Article
- SARS-CoV-2 proteins structural studies using synchrotron radiation.Biophysical reviews · 2023Review
- Changes in an Enzyme Ensemble During Catalysis Observed by High Resolution XFEL Crystallography.bioRxiv : the preprint server for biology · 2023Article
- FLEXR: automated multi-conformer model building using electron-density map sampling.Acta crystallographica. Section D, Structural biology · 2023Article
- Torsion angles to map and visualize the conformational space of a protein.Protein science : a publication of the Protein Society · 2023Article
- Microfluidic rotating-target device capable of three-degrees-of-freedom motion for efficient in situ serial synchrotron crystallography.Journal of synchrotron radiation · 2023Article
- Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature.IUCrJ · 2022Article
- Article
- Evaluating the impact of X-ray damage on conformational heterogeneity in room-temperature (277 K) and cryo-cooled protein crystals.Acta crystallographica. Section D, Structural biology · 2022Article
- Probing ligand binding of endothiapepsin by `temperature-resolved' macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2022Article
- Quantifying and comparing radiation damage in the Protein Data Bank.Nature communications · 2022Article
- An automated platform for structural analysis of membrane proteins through serial crystallography.Cell reports methods · 2021Article
- Temperature artifacts in protein structures bias ligand-binding predictions.Chemical science · 2021Article
- A SAXS-based approach to rationally evaluate radical scavengers - toward eliminating radiation damage in solution and crystallographic studies.Journal of synchrotron radiation · 2021Article
- Proline/arginine dipeptide repeat polymers derail protein folding in amyotrophic lateral sclerosis.Nature communications · 2021Article
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6 authors at 1 institution in 1 country.
Funding
Abstract
Protein crystallography data collection at synchrotrons is routinely carried out at cryogenic temperatures to mitigate radiation damage. Although damage still takes place at 100 K and below, the immobilization of free radicals increases the lifetime of the crystals by approximately 100-fold. Recent studies have shown that flash-cooling decreases the heterogeneity of the conformational ensemble and can hide important functional mechanisms from observation. These discoveries have motivated increasing numbers of experiments to be carried out at room temperature. However, the trade-offs between increased risk of radiation damage and increased observation of alternative conformations at room temperature relative to cryogenic temperature have not been examined. A considerable amount of effort has previously been spent studying radiation damage at cryo-temperatures, but the relevance of these studies to room temperature diffraction is not well understood. Here, the effects of radiation damage on the conformational landscapes of three different proteins (T. danielli thaumatin, hen egg-white lysozyme and human cyclophilin A) at room (278 K) and cryogenic (100 K) temperatures are investigated. Increasingly damaged datasets were collected at each temperature, up to a maximum dose of the order of 10
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.