ArticleActa crystallographica. Section D, Structural biology2018
Maximum-likelihood determination of anomalous substructures.
Article in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Observation of the Assembly of the Nascent Mineral Core at the Nucleation Site of Human Mitochondrial Ferritin.Journal of the American Chemical Society · 2025Article
- Structural insights into plasmalemma vesicle-associated protein (PLVAP): Implications for vascular endothelial diaphragms and fenestrae.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- How far are we from automatic crystal structure solution via molecular-replacement techniques?Acta crystallographica. Section D, Structural biology · 2020Article
- An introduction to experimental phasing of macromolecules illustrated by SHELX; new autotracing features.Acta crystallographica. Section D, Structural biology · 2018Article
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2 authors.
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Abstract
A fast Fourier transform (FFT) method is described for determining the substructure of anomalously scattering atoms in macromolecular crystals that allows successful structure determination by X-ray single-wavelength anomalous diffraction (SAD). This method is based on the maximum-likelihood SAD phasing function, which accounts for measurement errors and for correlations between the observed and calculated Bijvoet mates. Proof of principle is shown that this method can improve determination of the anomalously scattering substructure in challenging cases where the anomalous scattering from the substructure is weak but the substructure also constitutes a significant fraction of the real scattering. The method is deterministic and can be fast compared with existing multi-trial dual-space methods for SAD substructure determination.
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