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    Ab initio phasing of the diffraction of crystals with translational disorder

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    Author
    Morgan, AJ; Ayyer, K; Barty, A; Chen, JPJ; Ekeberg, T; Oberthuer, D; White, TA; Yefanov, O; Chapman, HN
    Date
    2019-01-01
    Source Title
    Acta Crystallographica Section A: Foundations and Advances
    Publisher
    INT UNION CRYSTALLOGRAPHY
    University of Melbourne Author/s
    Morgan, Andrew
    Affiliation
    School of Physics
    Metadata
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    Document Type
    Journal Article
    Citations
    Morgan, A. J., Ayyer, K., Barty, A., Chen, J. P. J., Ekeberg, T., Oberthuer, D., White, T. A., Yefanov, O. & Chapman, H. N. (2019). Ab initio phasing of the diffraction of crystals with translational disorder. ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 75 (Pt 1), pp.25-40. https://doi.org/10.1107/S2053273318015395.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/253388
    DOI
    10.1107/S2053273318015395
    Abstract
    To date X-ray protein crystallography is the most successful technique available for the determination of high-resolution 3D structures of biological molecules and their complexes. In X-ray protein crystallography the structure of a protein is refined against the set of observed Bragg reflections from a protein crystal. The resolution of the refined protein structure is limited by the highest angle at which Bragg reflections can be observed. In addition, the Bragg reflections alone are typically insufficient (by a factor of two) to determine the structure ab initio, and so prior information is required. Crystals formed from an imperfect packing of the protein molecules may also exhibit continuous diffraction between and beyond these Bragg reflections. When this is due to random displacements of the molecules from each crystal lattice site, the continuous diffraction provides the necessary information to determine the protein structure without prior knowledge, to a resolution that is not limited by the angular extent of the observed Bragg reflections but instead by that of the diffraction as a whole. This article presents an iterative projection algorithm that simultaneously uses the continuous diffraction as well as the Bragg reflections for the determination of protein structures. The viability of this method is demonstrated on simulated crystal diffraction.

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