ArticleActa crystallographica. Section D, Structural biology2022
Native SAD phasing at room temperature.
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 13 papers.
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13 citing papers in PubMed.
- Chaperonin recognition of protein dynamics drives drug resistance.bioRxiv : the preprint server for biology · 2026Article
- Sensitive detection of structural dynamics using a statistical framework for comparative crystallography.Science advances · 2025Article
- Laue-DIALS: Open-source software for polychromatic x-ray diffraction data.Structural dynamics (Melville, N.Y.) · 2024Article
- Sensitive Detection of Structural Differences using a Statistical Framework for Comparative Crystallography.bioRxiv : the preprint server for biology · 2024Article
- Laue-DIALS: open-source software for polychromatic X-ray diffraction data.bioRxiv : the preprint server for biology · 2024Article
- Article
- Perturbative diffraction methods resolve a conformational switch that facilitates a two-step enzymatic mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- MatchMaps: Non-isomorphous difference maps for X-ray crystallography.bioRxiv : the preprint server for biology · 2024Article
- 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
- Obtaining anomalous and ensemble information from protein crystals from 220 K up to physiological temperatures.Acta crystallographica. Section D, Structural biology · 2023Article
- Room-temperature serial synchrotron crystallography of the human phosphatase PTP1B.Acta crystallographica. Section F, Structural biology communications · 2023Article
- A unifying Bayesian framework for merging X-ray diffraction data.Nature communications · 2022Article
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6 authors.
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Abstract
Single-wavelength anomalous diffraction (SAD) is a routine method for overcoming the phase problem when solving macromolecular structures. This technique requires the accurate measurement of intensities to determine differences between Bijvoet pairs. Although SAD experiments are commonly conducted at cryogenic temperatures to mitigate the effects of radiation damage, such temperatures can alter the conformational ensemble of the protein and may impede the merging of data from multiple crystals due to non-uniform freezing. Here, a strategy is presented to obtain high-quality data from room-temperature, single-crystal experiments. To illustrate the strengths of this approach, native SAD phasing at 6.55 keV was used to solve four structures of three model systems at 295 K. The resulting data sets allow automatic phasing and model building, and reveal alternate conformations that reflect the structure of proteins at room temperature.
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