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Crystallization and preliminary X-ray diffraction analyses of the homodimeric glycine decarboxylase (P-protein) from the cyanobacterium Synechocystis sp PCC 6803

  • Dirk Hasse
  • , Martin Hagemann
  • , Inger Andersson
  • , Hermann Bauwe

    Publication: Contribution to journalJournal articlepeer-review

    Abstract

    Glycine decarboxylase or P-protein is a major enzyme involved in the C1 metabolism of all organisms and in the photorespiratory pathway of plants and cyanobacteria. The protein from Synechocystis sp. PCC 6803 is a homodimer with a mass of 215 kDa. Recombinant glycine decarboxylase was expressed in Escherichia coli and purified with metal affinity-, ion exchange- and gel filtration chromatography. Crystals of P-protein that diffracted to a resolution of 2.1 Å were obtained using the hanging drop vapour diffusion method at 291 K. X-ray diffraction data were collected from cryo-cooled crystals using synchrotron radiation. The crystals belong to space group P212121 with unit cell parameters a = 96.30 Å, b = 135.81 Å, and c = 179.08 Å
    Original languageEnglish
    Pages (from-to)187-191
    Number of pages5
    JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
    Volume66
    Issue number2
    DOIs
    Publication statusPublished - 2010

    Keywords

    • glycine decarboxylase
    • P-protein
    • crystallization

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