ArticleActa crystallographica. Section D, Biological crystallography2014
Improved crystal orientation and physical properties from single-shot XFEL stills.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Detector alignment for X-ray crystallography usingJournal of applied crystallography · 2026Article
- Evolution of macromolecular crystallography beamlines at the Swiss Light Source and SwissFEL.Journal of synchrotron radiation · 2025Article
- Serial-femtosecond crystallography reveals how a phytochrome variant couples chromophore and protein structural changes.Science advances · 2025Article
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- GARFIELD, a toolkit for interpreting ultrafast electron diffraction data of imperfect quasi-single crystals.Structural dynamics (Melville, N.Y.) · 2025Article
- 3D Nanocrystallography and the Imperfect Molecular Lattice.Annual review of physical chemistry · 2024Review
- In Situ Structural Observation of a Substrate- and Peroxide-Bound High-Spin Ferric-Hydroperoxo Intermediate in the P450 Enzyme CYP121.Journal of the American Chemical Society · 2023Article
- 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
- Serial femtosecond crystallography.Nature reviews. Methods primers · 2022Article
- X-ray free-electron laser studies reveal correlated motion during isopenicillinScience advances · 2021Article
- Beyond integration: modeling every pixel to obtain better structure factors from stills.IUCrJ · 2020Article
- Anaerobic fixed-target serial crystallography.IUCrJ · 2020Article
- Towards the spatial resolution of metalloprotein charge states by detailed modeling of XFEL crystallographic diffraction.Acta crystallographica. Section D, Structural biology · 2020Article
- SAD phasing of XFEL data depends critically on the error model.Acta crystallographica. Section D, Structural biology · 2019Article
- Data-driven challenges and opportunities in crystallography.Emerging topics in life sciences · 2019Article
- Unsupervised determination of protein crystal structures.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Nanoscale mosaicity revealed in peptide microcrystals by scanning electron nanodiffraction.Communications biology · 2019Article
- Improving signal strength in serial crystallography with DIALS geometry refinement.Acta crystallographica. Section D, Structural biology · 2018Article
- Serial Femtosecond Crystallography of G Protein-Coupled Receptors.Annual review of biophysics · 2018Review
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6 authors.
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Abstract
X-ray diffraction patterns from still crystals are inherently difficult to process because the crystal orientation is not uniquely determined by measuring the Bragg spot positions. Only one of the three rotational degrees of freedom is directly coupled to spot positions; the other two rotations move Bragg spots in and out of the reflecting condition but do not change the direction of the diffracted rays. This hinders the ability to recover accurate structure factors from experiments that are dependent on single-shot exposures, such as femtosecond diffract-and-destroy protocols at X-ray free-electron lasers (XFELs). Here, additional methods are introduced to optimally model the diffraction. The best orientation is obtained by requiring, for the brightest observed spots, that each reciprocal-lattice point be placed into the exact reflecting condition implied by Bragg's law with a minimal rotation. This approach reduces the experimental uncertainties in noisy XFEL data, improving the crystallographic R factors and sharpening anomalous differences that are near the level of the noise.
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