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

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

Keywords

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 and Nature Conservation
Forest Science

Publication identifier

• DOI: https://doi.org/10.1107/S1744309109052828

Permanent link to this page (URI)

https://res.slu.se/id/publ/28926