Crystallization and preliminary X-ray analysis of Streptococcus mutans dextran glucosidase.
Dextran glucosidase from Streptococcus mutans is an exo-hydrolase that acts on the nonreducing terminal alpha-1,6-glucosidic linkage of oligosaccharides and dextran with a high degree of transglucosylation. Based on amino-acid sequence similarity, this enzyme is classified into glycoside hydrolase family 13. Recombinant dextran glucosidase was purified and crystallized by the hanging-drop vapour-diffusion technique using polyethylene glycol 6000 as a precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 72.72, b = 86.47, c = 104.30 A. A native data set was collected to 2.2 A resolution from a single crystal.
Saburi
Wataru
W
Research Faculty of Agriculture, Hokkaido University, Sapporo, Hokkaido 060-8589, Japan.
Hondoh
Hironori
H
Unno
Hideaki
H
Okuyama
Masayuki
M
Mori
Haruhide
H
Nakada
Toshitaka
T
Matsuura
Yoshiki
Y
Kimura
Atsuo
A
D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D003911:Dextrans / Q000378:metabolism; D005959:Glucosidases / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D013295:Streptococcus mutans / Q000201:enzymology*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D003911:Dextrans; D011994:Recombinant Proteins; D005959:Glucosidases; C023149:exo-1,6-alpha-glucosidase