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  • Crystallization of DsbA, an Escherichia coli Protein Required for Disulphide Bond Formation in Vivo

    Author
    Martin, Jennifer L.
    Waksman, Gabriel
    Bardwell, James C.A.
    Beckwith, Jon
    Kuriyan, John
    Year published
    1993
    Metadata
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    Abstract
    DsbA is a 21 kDa protein that facilitates disulphide bond formation and is required for the correct folding and stability of a number of exported proteins in Escherichia coli. Crystals of oxidized DsbA have been obtained from polyethylene glycol 8000 (20 to 25% 0·1 M-cacodylate buffer (pH 6·5) and 1% 2-mehtyl-2,4-pentanediol. Oxidation of the protein is critical for reproducibly obtaining high quality crystals. The resulting crystals diffract to 2 Å and belong to the monoclinic space group C 2 with cel dimensions a=117·5 Å, b =65·0 Å, c76·3 Å, β=126·3° with two molecules in the asymmetric unit.DsbA is a 21 kDa protein that facilitates disulphide bond formation and is required for the correct folding and stability of a number of exported proteins in Escherichia coli. Crystals of oxidized DsbA have been obtained from polyethylene glycol 8000 (20 to 25% 0·1 M-cacodylate buffer (pH 6·5) and 1% 2-mehtyl-2,4-pentanediol. Oxidation of the protein is critical for reproducibly obtaining high quality crystals. The resulting crystals diffract to 2 Å and belong to the monoclinic space group C 2 with cel dimensions a=117·5 Å, b =65·0 Å, c76·3 Å, β=126·3° with two molecules in the asymmetric unit.
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    Journal Title
    Journal of Molecular Biology
    Volume
    230
    Issue
    3
    DOI
    https://doi.org/10.1006/jmbi.1993.1226
    Subject
    Biochemistry and Cell Biology not elsewhere classified
    Publication URI
    http://hdl.handle.net/10072/347918
    Collection
    • Journal articles

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