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Research article - Peer-reviewed, 2010

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

Authors' information

Hasse, Dirk
Hagemann, Martin
Andersson, Inger
Swedish University of Agricultural Sciences, Department of Molecular Biology
Bauwe, Hermann

UKÄ Subject classification

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

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