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

    Author(s)
    MARTIN, JL
    WAKSMAN, G
    BARDWELL, JCA
    BECKWITH, J
    KURIYAN, J
    Griffith University Author(s)
    Martin, Jennifer
    Year published
    1993
    Metadata
    Show full item record
    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
    Medicinal and biomolecular chemistry
    Biochemistry and cell biology
    Biochemistry and cell biology not elsewhere classified
    Microbiology
    Publication URI
    http://hdl.handle.net/10072/347918
    Collection
    • Journal articles

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