Crystallization and preliminary X-ray studies of glutathione synthetase from Escherichia coli B.
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.
Kato
H
H
Institute for Chemical Research, Kyoto University, Japan.
Yamaguchi
H
H
Hata
Y
Y
Nishioka
T
T
Katsube
Y
Y
Oda
J
J
D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D005981:Glutathione Synthase; D010453:Peptide Synthases; D014961:X-Ray Diffraction
D010453:Peptide Synthases; D005981:Glutathione Synthase