ArticleActa crystallographica. Section D, Biological crystallography2012
Outrunning free radicals in room-temperature macromolecular crystallography.
Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
65 citing papers in PubMed, 92 citations in OpenAlex.
- Snapshots of internal protein crystal architecture at the nanoscale.Biophysical journal · 2026Article
- Separating the effects of temperature and absorbed X-ray dose on unit-cell volume.Acta crystallographica. Section D, Structural biology · 2026Article
- Mapping the effects of specific radiation damage and solvent radiolysis in buffers and crystals with online UV-Vis absorption spectroscopy.Acta crystallographica. Section D, Structural biology · 2026Article
- Article
- Snapshots of Internal Protein Crystal Architecture at the Nanoscale.bioRxiv : the preprint server for biology · 2026Article
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Evolution of macromolecular crystallography beamlines at the Swiss Light Source and SwissFEL.Journal of synchrotron radiation · 2025Article
- Cryo2RT: a high-throughput method for room-temperature macromolecular crystallography from cryo-cooled crystals.Acta crystallographica. Section D, Structural biology · 2024Article
- Doses for X-ray and electron diffraction: New features in RADDOSE-3D including intensity decay models.Protein science : a publication of the Protein Society · 2024Article
- Power Density Titration of Reversible Photoisomerization of a Fluorescent Protein Chromophore in the Presence of Thermally Driven Barrier Crossing Shown by Quantitative Millisecond Serial Synchrotron X-ray Crystallography.Journal of the American Chemical Society · 2024Article
- Identifying and avoiding radiation damage in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2024Article
- X-ray driven and intrinsic dynamics in protein gels.Scientific reports · 2023Article
- Variability in X-ray induced effects in [Rh(COD)Cl]Physical chemistry chemical physics : PCCP · 2022Article
- Megahertz pulse trains enable multi-hit serial femtosecond crystallography experiments at X-ray free electron lasers.Nature communications · 2022Article
- Probing ligand binding of endothiapepsin by `temperature-resolved' macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2022Article
- 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
- xia2.multiplex: a multi-crystal data-analysis pipeline.Acta crystallographica. Section D, Structural biology · 2022Article
- A SAXS-based approach to rationally evaluate radical scavengers - toward eliminating radiation damage in solution and crystallographic studies.Journal of synchrotron radiation · 2021Article
- Pushing the limits of high-resolution polymer microscopy using antioxidants.Nature communications · 2021Article
- Instrumentation and experimental procedures for robust collection of X-ray diffraction data from protein crystals across physiological temperatures.Journal of applied crystallography · 2020Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 7 institutions in 3 countries.
Funding
Abstract
A significant increase in the lifetime of room-temperature macromolecular crystals is reported through the use of a high-brilliance X-ray beam, reduced exposure times and a fast-readout detector. This is attributed to the ability to collect diffraction data before hydroxyl radicals can propagate through the crystal, fatally disrupting the lattice. Hydroxyl radicals are shown to be trapped in amorphous solutions at 100 K. The trend in crystal lifetime was observed in crystals of a soluble protein (immunoglobulin γ Fc receptor IIIa), a virus (bovine enterovirus serotype 2) and a membrane protein (human A(2A) adenosine G-protein coupled receptor). The observation of a similar effect in all three systems provides clear evidence for a common optimal strategy for room-temperature data collection and will inform the design of future synchrotron beamlines and detectors for macromolecular crystallography.
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Registered trials
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.