Open AccessCrystallization and preliminary X‐ray diffraction analyses of the homodimeric glycine decarboxylase (P‐protein) from the cyanobacterium Synechocystis sp. PCC 6803
Author(s) -
Hasse Dirk,
Hagemann Martin,
Andersson Inger,
Bauwe Hermann
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109052828
Subject(s) - synechocystis , cyanobacteria , glycine , crystallization , chemistry , crystallography , x ray crystallography , diffraction , biochemistry , biology , physics , bacteria , amino acid , organic chemistry , optics , genetics
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 Å 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 P 2 1 2 1 2 1 , with unit‐cell parameters a = 96.30, b = 135.81, c = 179.08 Å.