ArticleeLife2015
Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
83 citing papers in PubMed.
- Generation and modulation of catalytically relevant states of a dye-decolourizing peroxidase using time-resolved serial femtosecond crystallography with drop-on-chip mixing and X-ray-driven reduction.Acta crystallographica. Section D, Structural biology · 2026Article
- Detector alignment for X-ray crystallography usingJournal of applied crystallography · 2026Article
- Sensitive detection of structural dynamics using a statistical framework for comparative crystallography.Science advances · 2025Article
- Article
- Sensitive Detection of Structural Differences using a Statistical Framework for Comparative Crystallography.bioRxiv : the preprint server for biology · 2024Article
- 3D Nanocrystallography and the Imperfect Molecular Lattice.Annual review of physical chemistry · 2024Review
- Correcting systematic errors in diffraction data with modern scaling algorithms.Acta crystallographica. Section D, Structural biology · 2023Article
- The CCP4 suite: integrative software for macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2023Article
- Emerging Time-Resolved X-Ray Diffraction Approaches for Protein Dynamics.Annual review of biophysics · 2023Review
- Article
- Interpreting macromolecular diffraction through simulation.Methods in enzymology · 2023Article
- Sample Preparation for Time-Resolved Serial Crystallography: Practical Considerations.Methods in molecular biology (Clifton, N.J.) · 2023Article
- A unifying Bayesian framework for merging X-ray diffraction data.Nature communications · 2022Article
- Linking scientific instruments and computation: Patterns, technologies, and experiences.Patterns (New York, N.Y.) · 2022Article
- Fixed-target serial crystallography at the Structural Biology Center.Journal of synchrotron radiation · 2022Article
- Serial femtosecond crystallography.Nature reviews. Methods primers · 2022Article
- De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals.Nature communications · 2022Article
- Plug-and-play polymer microfluidic chips for hydrated, room temperature, fixed-target serial crystallography.Lab on a chip · 2021Article
- X-ray free-electron laser studies reveal correlated motion during isopenicillinScience advances · 2021Article
- 2'-O methylation of RNA cap in SARS-CoV-2 captured by serial crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
23 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
8 authors.
Funding
Abstract
There is considerable potential for X-ray free electron lasers (XFELs) to enable determination of macromolecular crystal structures that are difficult to solve using current synchrotron sources. Prior XFEL studies often involved the collection of thousands to millions of diffraction images, in part due to limitations of data processing methods. We implemented a data processing system based on classical post-refinement techniques, adapted to specific properties of XFEL diffraction data. When applied to XFEL data from three different proteins collected using various sample delivery systems and XFEL beam parameters, our method improved the quality of the diffraction data as well as the resulting refined atomic models and electron density maps. Moreover, the number of observations for a reflection necessary to assemble an accurate data set could be reduced to a few observations. These developments will help expand the applicability of XFEL crystallography to challenging biological systems, including cases where sample is limited.
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