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    Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt 9):917-9. Epub 2009 Aug 22.

    Crystallization and preliminary X-ray crystallographic analysis of PhoK, an extracellular alkaline phosphatase from Sphingomonas sp. BSAR-1.

    Source

    Molecular Biology Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400085, India.

    Abstract

    Alkaline phosphatases (APs) are widely distributed from microbes to humans and are involved in several important biological processes such as phosphate nutrition, signal transduction and pathogenesis. Alkaline phosphatases are also useful in various industrial applications and in recombinant DNA technology. A new AP enzyme from Sphingomonas sp. strain BSAR-1, termed PhoK, has been shown to be useful in uranium bioprecipitation. PhoK was expressed, purified and crystallized. The crystals belonged to space group P4(3)2(1)2 or P4(1)2(1)2, with unit-cell parameters a = b = 87.37, c = 168.16 A, and contained one enzyme molecule in the asymmetric unit. Native diffraction data have been collected to 1.95 A resolution at the ESRF.

    PMID:
    19724132
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2795600
    Free PMC Article

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