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  • Crystallization of a novel a-amylase, AmyB, from the thermophilic halophile Halothermothrix orenii

    Author(s)
    Tan, Tien-Chye
    Y. Yien, Yvette
    Patel, Bharat
    Mijts, Benjamin
    Swaminathan, Kunchithapadam
    Griffith University Author(s)
    Patel, Bharat K.
    Mijts, Benjamin
    Year published
    2003
    Metadata
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    Abstract
    This is a report on the structure determination of AmyB, the second a-amylase from Halothermothrix orenii, by X-ray crystallography. This bacterium was isolated from saltpans where conditions consisted of both high temperatures and high NaCl content. AmyB is a 599-�sidue protein which is stable and significantly active at 358 K in starch solution containing up to 10%(w/v) NaCl. The purified recombinant AmyB protein crystallizes in the monoclinic space group C2, with unit-cell parameters a = 225.85, b = 77.16, c = 50.13 Ŭ ߠ= 99.32ଠusing the hanging-drop vapour-diffusion method. The crystal diffracts X-�ys to a resolution ...
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    This is a report on the structure determination of AmyB, the second a-amylase from Halothermothrix orenii, by X-ray crystallography. This bacterium was isolated from saltpans where conditions consisted of both high temperatures and high NaCl content. AmyB is a 599-�sidue protein which is stable and significantly active at 358 K in starch solution containing up to 10%(w/v) NaCl. The purified recombinant AmyB protein crystallizes in the monoclinic space group C2, with unit-cell parameters a = 225.85, b = 77.16, c = 50.13 Ŭ ߠ= 99.32ଠusing the hanging-drop vapour-diffusion method. The crystal diffracts X-�ys to a resolution limit of 1.97 Ů
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    Journal Title
    Acta Crystallographica, Section D: Biological Crystallography
    Volume
    D59
    Publisher URI
    http://www.blackwell-synergy.com/doi/full/10.1107/S0907444903018754
    DOI
    https://doi.org/10.1107/S0907444903018754
    Subject
    Physical Sciences
    Chemical Sciences
    Biological Sciences
    Publication URI
    http://hdl.handle.net/10072/6289
    Collection
    • Journal articles

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