Open AccessCrystallization and preliminary X‐ray analysis of Streptococcus mutans dextran glucosidase
Author(s) -
Saburi Wataru,
Hondoh Hironori,
Unno Hideaki,
Okuyama Masayuki,
Mori Haruhide,
Nakada Toshitaka,
Matsuura Yoshiki,
Kimura Atsuo
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910703936x
Subject(s) - dextran , streptococcus mutans , orthorhombic crystal system , crystallization , polyethylene glycol , hydrolase , glycoside hydrolase , chemistry , enzyme , crystallography , biochemistry , crystal structure , bacteria , biology , organic chemistry , genetics
Dextran glucosidase from Streptococcus mutans is an exo‐hydrolase that acts on the nonreducing terminal α‐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 P 2 1 2 1 2 1 , with unit‐cell parameters a = 72.72, b = 86.47, c = 104.30 Å. A native data set was collected to 2.2 Å resolution from a single crystal.