Crystallization and preliminary crystallographic analysis of bacterial fructosyl amino acid oxidase.
Bacterial fructosyl amino acid oxidase [fructosyl alpha-L-amino acid:oxygen oxidoreductase (defructosylating); EC 1.5.3] has been crystallized by the hanging-drop vapour-diffusion technique using sodium citrate as the precipitant. Two types of crystals were grown: one type are rhombic prismatic yellow crystals that belong to space group C2 with unit-cell parameters a = 101.08, b = 63.36, c = 83.07 A, beta = 108.80 degrees and diffract to at least 1.8 A resolution, while the second type are rod-like crystals that belong to space group P4(1)22 or P4(3)22 with unit-cell parameters a = b = 119.09, c = 164.66 A and diffract to 2.7 A resolution.
Sakaue
Ryoichi
R
Research and Development Division, Kikkoman Corporation, 399 Noda, Noda City, Chiba 278-0037, Japan.
Nakatsu
Toru
T
Yamaguchi
Yoko
Y
Kato
Hiroaki
H
Kajiyama
Naoki
N
D000594:Amino Acid Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D000594:Amino Acid Oxidoreductases; C103012:amadoriase