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Escherichia coli B gamma-glutamylcysteine synthetase: modification, purification, crystallization and preliminary
Takao Hibi1, Hiromoto Hisada, Toru Nakatsu
1Department of Bioscience, Fukui Prefectural University, Fukui 910-1195, Japan. hibi@fpu.ac.jp
Acta Crystallographica. Section D, Biological Crystallography
|January 25, 2002
Abstract:
Escherichia coli B gamma-glutamylcysteine synthetase (gammaGCS) catalyzes the ATP-dependent coupling of L-Glu and L-Cys to form the glutathione precursor gamma-L-Glu-Cys and is a target for development of potential therapeutic agents. By introducing four point mutations of surface-exposed cysteine residues to serine, the gammaGCS was purified to homogeneity; single crystals have been obtained using the hanging-drop vapour-diffusion method with sodium formate. The gammaGCS crystal diffracted to 2.8 A and belongs to space group R3, with unit-cell parameters a = b = 326.7, c = 103.9 A.