title: Three-dimensional structure of aspartate aminotransferase from Escherichia coli at 2.8 A resolution.
abstract: The crystal structure of aspartate aminotransferase of Escherichia coli was determined by X-ray structure analysis at 2.8 A resolution. The structure was solved by the molecular replacement method and refined to an R-factor of 0.27, and it was found that the overall structure of AspAT of E. coli is similar to that of those of higher animals.
authors.affiliation: Department of Chemistry, Faculty of Science, Osaka City University.
authors.forename: S
authors.initials: S
authors.lastname: Kamitori
authors.forename: K
authors.initials: K
authors.lastname: Hirotsu
authors.forename: T
authors.initials: T
authors.lastname: Higuchi
authors.forename: K
authors.initials: K
authors.lastname: Kondo
authors.forename: K
authors.initials: K
authors.lastname: Inoue
authors.forename: S
authors.initials: S
authors.lastname: Kuramitsu
authors.forename: H
authors.initials: H
authors.lastname: Kagamiyama
authors.forename: Y
authors.initials: Y
authors.lastname: Higuchi
authors.forename: N
authors.initials: N
authors.lastname: Yasuoka
authors.forename: M
authors.initials: M
authors.lastname: Kusunoki
mesh_terms: D001219:Aspartate Aminotransferases; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D001219:Aspartate Aminotransferases