Maximum-likelihood determination of anomalous substructures.
Acta crystallographica. Section D, Structural biology
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Read, R., & McCoy, A. (2018). Maximum-likelihood determination of anomalous substructures.. Acta crystallographica. Section D, Structural biology, 74 (Pt 2), 98-105. https://doi.org/10.1107/s2059798317013468
We describe an FFT method 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. We show proof of principle 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 to existing multi-trial dual-space methods for SAD substructure determination.
Chick Embryo, Animals, Macromolecular Substances, Muramidase, Carbamoyl-Phosphate Synthase (Ammonia), Bacterial Proteins, Ferredoxins, Crystallography, X-Ray, Likelihood Functions, Protein Conformation, Fourier Analysis, Thioredoxins
Wellcome Trust (082961/Z/07/A)
Wellcome Trust (082961/Z/07/Z)
Wellcome Trust (100140/Z/12/Z)
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External DOI: https://doi.org/10.1107/s2059798317013468
This record's URL: https://www.repository.cam.ac.uk/handle/1810/275503
Attribution 4.0 International, Attribution 4.0 International, Attribution 4.0 International, Attribution 4.0 International