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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):187-91. doi: 10.1107/S1744309109052828. Epub 2010 Jan 28.

Abstract

Glycine decarboxylase, or P-protein, is a major enzyme that is involved in the C(1) 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 by metal-affinity, ion-exchange and gel-filtration chromatography. Crystals of P-protein that diffracted to a resolution of 2.1 A were obtained using the hanging-drop vapour-diffusion method at 291 K. X-ray diffraction data were collected from cryocooled crystals using synchrotron radiation. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 96.30, b = 135.81, c = 179.08 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallization
  • Glycine Dehydrogenase (Decarboxylating) / chemistry*
  • Glycine Dehydrogenase (Decarboxylating) / genetics
  • Glycine Dehydrogenase (Decarboxylating) / metabolism
  • Humans
  • Phylogeny
  • Protein Multimerization*
  • Synechocystis / enzymology*
  • X-Ray Diffraction

Substances

  • Glycine Dehydrogenase (Decarboxylating)