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Maximum-likelihood determination of anomalous substructures.

Published version
Peer-reviewed

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Authors

McCoy, Airlie J 

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.

Description

Keywords

likelihood, single-wavelength anomalous diffraction, substructure determination, Animals, Bacterial Proteins, Carbamoyl-Phosphate Synthase (Ammonia), Chick Embryo, Crystallography, X-Ray, Ferredoxins, Fourier Analysis, Likelihood Functions, Macromolecular Substances, Muramidase, Protein Conformation, Thioredoxins

Journal Title

Acta Crystallogr D Struct Biol

Conference Name

Journal ISSN

2059-7983
2059-7983

Volume Title

74

Publisher

International Union of Crystallography (IUCr)
Sponsorship
Wellcome Trust (082961/Z/07/A)
Biotechnology and Biological Sciences Research Council (BB/L006014/1)
Wellcome Trust (082961/Z/07/Z)
Wellcome Trust (100140/Z/12/Z)
Wellcome Trust (209407/Z/17/Z)