Crystallization and preliminary X-ray studies of glutathione synthetase from Escherichia coli B

• Published in: Journal of molecular biology Vol. 209; no. 3; p. 503
• Main Authors: Kato, H, Yamaguchi, H, Hata, Y, Nishioka, T, Katsube, Y, Oda, J
• Format: Journal Article
• Language: English
• Published: England 05-10-1989
• Subjects: Crystallization; Escherichia coli - enzymology; Glutathione Synthase; Peptide Synthases; X-Ray Diffraction
• ISSN: 0022-2836
• DOI: 10.1016/0022-2836(89)90015-6

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.