ArticleIUCrJ2018
Intermolecular correlations are necessary to explain diffuse scattering from protein crystals.
Article in IUCrJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Scaling and merging macromolecular diffuse scattering with mdx2.Acta crystallographica. Section D, Structural biology · 2024Article
- Scaling and merging macromolecular diffuse scattering withbioRxiv : the preprint server for biology · 2024Article
- Processing macromolecular diffuse scattering data.bioRxiv : the preprint server for biology · 2023Article
- Robust total X-ray scattering workflow to study correlated motion of proteins in crystals.Nature communications · 2023Article
- Interpreting macromolecular diffraction through simulation.Methods in enzymology · 2023Article
- Correlated Motions in Structural Biology.Biochemistry · 2021Review
- Reproducibility of protein x-ray diffuse scattering and potential utility for modeling atomic displacement parameters.Structural dynamics (Melville, N.Y.) · 2021Article
- Diffuse X-ray scattering from correlated motions in a protein crystal.Nature communications · 2020Article
- Transactions from the 69th Annual Meeting of the American Crystallographic Association: Data best practices-current state and future needs.Structural dynamics (Melville, N.Y.) · 2020Review
- Liquid-like and rigid-body motions in molecular-dynamics simulations of a crystalline protein.Structural dynamics (Melville, N.Y.) · 2019Article
- Transforming X-ray detection with hybrid photon counting detectors.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2019Article
- Article
- Bringing diffuse X-ray scattering into focus.Current opinion in structural biology · 2018Review
- Interactions that know no boundaries.IUCrJ · 2018Article
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Authors and funding
3 authors.
Funding
Abstract
Conformational changes drive protein function, including catalysis, allostery and signaling. X-ray diffuse scattering from protein crystals has frequently been cited as a probe of these correlated motions, with significant potential to advance our understanding of biological dynamics. However, recent work has challenged this prevailing view, suggesting instead that diffuse scattering primarily originates from rigid-body motions and could therefore be applied to improve structure determination. To investigate the nature of the disorder giving rise to diffuse scattering, and thus the potential applications of this signal, a diverse repertoire of disorder models was assessed for its ability to reproduce the diffuse signal reconstructed from three protein crystals. This comparison revealed that multiple models of intramolecular conformational dynamics, including ensemble models inferred from the Bragg data, could not explain the signal. Models of rigid-body or short-range liquid-like motions, in which dynamics are confined to the biological unit, showed modest agreement with the diffuse maps, but were unable to reproduce experimental features indicative of long-range correlations. Extending a model of liquid-like motions to include disorder across neighboring proteins in the crystal significantly improved agreement with all three systems and highlighted the contribution of intermolecular correlations to the observed signal. These findings anticipate a need to account for intermolecular disorder in order to advance the interpretation of diffuse scattering to either extract biological motions or aid structural inference.
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