Crystallization and preliminary X-ray characterization of branched-chain amino acid aminotransferase from Escherichia coli.
The branched-chain amino acid aminotransferase of Escherichia coli was crystallized in two crystal systems, monoclinic and tetragonal, from polyethylene glycol and ammonium sulfate solutions, pH 7.0, respectively. The crystals were of good quality, with diffractions extending beyond 2.8 A. The space group and unit cell dimensions of the monoclinic system crystals were determined from precession photographs to be C2, and a = 93.9, b = 143.6, c = 143.9 A and beta = 134.3 degrees. For the tetragonal system crystals, the possible space group P422 or P4122, and cell dimensions of a = b = 101 A and c = 249 A were determined. Three identical subunits exist per an asymmetric unit in both types of crystals.
Kamitori
S
S
Department of Chemistry, Faculty of Science, Osaka City University.
Odagaki
Y
Y
Inoue
K
K
Kuramitsu
S
S
Kagamiyama
H
H
Matsuura
Y
Y
Higuchi
T
T
D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation; D000637:Transaminases / Q000032:analysis / Q000302:isolation & purification*; D014961:X-Ray Diffraction
D000637:Transaminases; C019798:branched-chain-amino-acid transaminase