Crystallization and preliminary X-ray diffraction analyses of the homodimeric glycine decarboxylase (P-protein) from the cyanobacterium Synechocystis sp. PCC 6803.
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.
Hasse
Dirk
D
Department of Plant Physiology, University of Rostock, Germany.
Hagemann
Martin
M
Andersson
Inger
I
Bauwe
Hermann
H
D000818:Animals; D003460:Crystallization; D050841:Glycine Dehydrogenase (Decarboxylating) / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D010802:Phylogeny; D055503:Protein Multimerization; D046939:Synechocystis / Q000201:enzymology*; D014961:X-Ray Diffraction
D050841:Glycine Dehydrogenase (Decarboxylating)