Crystallization and preliminary X-ray crystallographic studies of alpha-galactosidase I from Mortierella vinacea.
alpha-Galactosidases catalyze the hydrolysis of a galactosyl residue from galactooligosaccharides and galactopolysaccharides. alpha-Galactosidase I from Mortierella vinacea was crystallized in two crystal forms using the hanging-drop vapour-diffusion method. Type 1 crystals belonged to space group I422, with unit-cell parameters a = b = 142.4, c = 131.5 A, and diffracted to beyond 2.1 A resolution, while type 2 crystals belonged to space group P4, with unit-cell parameters a = b = 100.9, c = 102.7 A, and diffracted to beyond 1.6 A resolution. This enzyme crystallized as a glycoprotein tetramer and the tetrameric structure was located around the crystallographic fourfold axis.
Fujimoto
Zui
Z
Department of Biochemistry, National Institute of Agrobiological Sciences, Tsukuba 305-8602, Japan.
Kim
Wook-Dong
WD
Kaneko
Satoshi
S
Park
Gwi-Gun
GG
Momma
Mitsuru
M
Kobayashi
Hideyuki
H
Mizuno
Hiroshi
H
D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry; D020094:Mortierella / Q000201:enzymology*; D020836:Protein Structure, Quaternary; D000519:alpha-Galactosidase / Q000737:chemistry*
D001426:Bacterial Proteins; D005656:Fungal Proteins; C115462:alpha-galactosidase I; D000519:alpha-Galactosidase