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    Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jan 1;64(Pt 1):36-8. Epub 2007 Dec 20.

    Overproduction, crystallization and preliminary X-ray analysis of the putative L-ascorbate-6-phosphate lactonase UlaG from Escherichia coli.

    Garces F, Fernández FJ, Pérez-Luque R, Aguilar J, Baldomà L, Coll M, Badía J, Vega MC.

    Source

    Structural Biology Department, Institut de Biologia Molecular de Barcelona and Institut de Recerca Biomèdica, E-08028 Barcelona, Spain.

    Abstract

    UlaG, the putative L-ascorbate-6-phosphate lactonase encoded by the ulaG gene from the utilization of L-ascorbate regulon in Escherichia coli, has been cloned, overexpressed, purified using standard chromatographic techniques and crystallized. Crystals were obtained by sitting-drop vapour diffusion at 293 K. Preliminary X-ray diffraction analysis revealed that the UlaG crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 104.52, b = 180.69, c = 112.88 A, beta = 103.26 degrees. The asymmetric unit is expected to contain six copies of UlaG, with a corresponding volume per protein weight of 2.16 A3 Da(-1) and a solvent content of 43%.

    PMID:
    18097099
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2373999
    Free PMC Article

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