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Research article2010Peer reviewedOpen access

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

Hasse Dirk, Hagemann Martin, Andersson Inger, Bauwe Hermann


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


glycine decarboxylase; P-protein; crystallization

Published in

Acta Crystallographica Section F: Structural Biology and Crystallization Communications
2010, Volume: 66, number: 2, pages: 187-191
Publisher: Wiley

      SLU Authors

    • Andersson, Inger

      • Department of Molecular Biology, Swedish University of Agricultural Sciences

    UKÄ Subject classification

    Agricultural Science
    Environmental Sciences related to Agriculture and Land-use
    Forest Science

    Publication identifier


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