title: Crystallization and preliminary X-ray studies of glutathione synthetase from Escherichia coli B.
abstract: The glutathione synthetase from Escherichia coli B has been crystallized from 27% saturated ammonium sulfate solution (pH 5.5). The crystals are hexagonal, space group P6(2)22 or P6(4)22. The cell dimensions are a = b = 88.0 A, c = 164.2 A, and gamma = 120 degrees. The enzyme is a tetramer (Mr = 143,000) with 222 symmetry, and the asymmetric unit contains one subunit molecule (Mr = 35,600). The crystals diffract to at least 2.5 A resolution.
authors.affiliation: Institute for Chemical Research, Kyoto University, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Kato
authors.forename: H
authors.initials: H
authors.lastname: Yamaguchi
authors.forename: Y
authors.initials: Y
authors.lastname: Hata
authors.forename: T
authors.initials: T
authors.lastname: Nishioka
authors.forename: Y
authors.initials: Y
authors.lastname: Katsube
authors.forename: J
authors.initials: J
authors.lastname: Oda
mesh_terms: D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D005981:Glutathione Synthase; D010453:Peptide Synthases; D014961:X-Ray Diffraction
chemical_list: D010453:Peptide Synthases; D005981:Glutathione Synthase