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Expression, purification and preliminary diffraction studies of PhnP

  • Kateryna Podzelinska
  • , Shu-Mei He
  • , Alexei Soares
  • , David L. Zechel
  • , Bjarne Hove-Jensen
  • , Zongchao Jia
    • Queen's University
    • Department of Biology, Brookhaven National Laboratory, Upton
    • University of Copenhagen

    Research output: Contribution to journal › Journal article › Research › peer-review

    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 Å and the crystals belonged to space group C2, with unit-cell parameters a = 111.65, b = 75.41, c = 83.23 Å, α = γ = 90, β = 126.3°.

    Original languageEnglish
    JournalActa Crystallographica. Section F: Structural Biology and Crystallization Communications Online
    Volume64
    Issue number6
    Pages (from-to)554-557
    Number of pages4
    ISSN1744-3091
    DOIs
    Publication statusPublished - 2008

    Keywords

    • C-P lyases
    • Organophosphonate metabolism
    • PhnP

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