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    Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt 6):554-7. doi: 10.1107/S1744309108014656. Epub 2008 May 24.

    Expression, purification and preliminary diffraction studies of PhnP.

    Source

    Department of Biochemistry, Queen's University, Kingston K7L 3N6, Canada.

    Abstract

    PhnP belongs to a 14-gene operon that supports the growth of Escherichia coli on alkylphosphonates as a sole source of phosphorus; however, the exact biochemistry of phosphonate degradation by this pathway is poorly understood. The protein was recombinantly expressed in Escherichia coli and purified to homogeneity. Sitting-drop vapour diffusion in combination with microseeding was used to obtain crystals that were suitable for X-ray diffraction. Data were collected to 1.3 A and the crystals belonged to space group C2, with unit-cell parameters a = 111.65, b = 75.41, c = 83.23 A, alpha = gamma = 90, beta = 126.3 degrees .

    PMID:
    18540074
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2496866
    Free PMC Article

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