title: Crystallization and preliminary X-ray crystallographic studies of alpha-galactosidase I from Mortierella vinacea.
abstract: 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.
authors.affiliation: Department of Biochemistry, National Institute of Agrobiological Sciences, Tsukuba 305-8602, Japan.
authors.forename: Zui
authors.initials: Z
authors.lastname: Fujimoto
authors.forename: Wook-Dong
authors.initials: WD
authors.lastname: Kim
authors.forename: Satoshi
authors.initials: S
authors.lastname: Kaneko
authors.forename: Gwi-Gun
authors.initials: GG
authors.lastname: Park
authors.forename: Mitsuru
authors.initials: M
authors.lastname: Momma
authors.forename: Hideyuki
authors.initials: H
authors.lastname: Kobayashi
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Mizuno
mesh_terms: 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*
chemical_list: D001426:Bacterial Proteins; D005656:Fungal Proteins; C115462:alpha-galactosidase I; D000519:alpha-Galactosidase