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  • Expression, purification and preliminary crystallographic analysis of sucrose phosphate synthase (SPS) from Halothermothrix orenii. .

    Author(s)
    Huynh, Frederick
    Tan, Tien-Chye
    Swaminathan, Kunchithapadam
    Patel, Bharat KC
    Griffith University Author(s)
    Patel, Bharat K.
    Huynh, Frederick
    Year published
    2005
    Metadata
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    Abstract
    This is the first report of the crystallization of a sucrose phosphate synthase (SPS; EC 2.4.1.14). It also constitutes the first study of a sucrose phosphate synthase from a non-photosynthetic thermohalophilic anaerobic bacterium, Halothermothrix orenii. The purified recombinant spsA protein has been crystallized in the monoclinic space group C2, with unit-cell parameters a = 154.2, b = 47.9, c = 72.3 Ŭ = 103.16ଠusing the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 3.01 Ů Heavy-metal and halide-soaking trials are currently in progress to solve the structure.This is the first report of the crystallization of a sucrose phosphate synthase (SPS; EC 2.4.1.14). It also constitutes the first study of a sucrose phosphate synthase from a non-photosynthetic thermohalophilic anaerobic bacterium, Halothermothrix orenii. The purified recombinant spsA protein has been crystallized in the monoclinic space group C2, with unit-cell parameters a = 154.2, b = 47.9, c = 72.3 Ŭ = 103.16ଠusing the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 3.01 Ů Heavy-metal and halide-soaking trials are currently in progress to solve the structure.
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    Journal Title
    Acta Crystallograph Section F Structrural Biology and Crystallization Communications
    Volume
    F61
    Publisher URI
    http://journals.iucr.org/f/issues/2005/01/00/ll5007/index.html
    DOI
    https://doi.org/10.1107/S174430910403091X
    Subject
    Chemical Sciences
    Biological Sciences
    Publication URI
    http://hdl.handle.net/10072/4902
    Collection
    • Journal articles

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