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  • Expression, purification and preliminary crystallographic analysis of the recombinant β- glucosidase (BglA) from halothermophile Halothermothrix orenii

    Author(s)
    Kori, Lokesh D
    Hofmann, Andreas
    Patel, Bharat KC
    Griffith University Author(s)
    Patel, Bharat K.
    Hofmann, Andreas
    Kori, Lokesh
    Year published
    2011
    Metadata
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    Abstract
    The [beta]-glucosidase A gene (bglA) has been cloned from the halothermophilic bacterium Halothermothrix orenii and the recombinant enzyme (BglA; EC 3.2.1.21) was bacterially expressed, purified using metal ion-affinity chromatography and subsequently crystallized. Orthorhombic crystals were obtained that diffracted to a resolution limit of 3.5 Ů The crystal structure with two molecules in the asymmetric unit was solved by molecular replacement using a library of known glucosidase structures. Attempts to collect higher resolution diffraction data from crystals grown under different conditions and structure refinement are ...
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    The [beta]-glucosidase A gene (bglA) has been cloned from the halothermophilic bacterium Halothermothrix orenii and the recombinant enzyme (BglA; EC 3.2.1.21) was bacterially expressed, purified using metal ion-affinity chromatography and subsequently crystallized. Orthorhombic crystals were obtained that diffracted to a resolution limit of 3.5 Ů The crystal structure with two molecules in the asymmetric unit was solved by molecular replacement using a library of known glucosidase structures. Attempts to collect higher resolution diffraction data from crystals grown under different conditions and structure refinement are currently in progress.
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    Journal Title
    Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online
    Volume
    F67
    Issue
    1
    Publisher URI
    https://journals.iucr.org/f/issues/2011/01/00/
    Subject
    Chemical sciences
    Biological sciences
    Structural biology (incl. macromolecular modelling)
    Publication URI
    http://hdl.handle.net/10072/39782
    Collection
    • Journal articles

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