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Title: Crystallization and preliminary X-ray analysis of Streptococcus mutans dextran glucosidase

Journal Article · · Acta Crystallographica. Section F
;  [1];  [2]; ;  [1];  [3];  [4];  [1]
  1. Research Faculty of Agriculture, Hokkaido University, Sapporo, Hokkaido 060-8589 (Japan)
  2. Faculty of Engineering, Nagasaki University, Bunkyo-machi, Nagasaki 852-8521 (Japan)
  3. Faculty of Science and Engineering, Ritsumeikan University, Kusatsu, Shiga 525-8577 (Japan)
  4. Institute for Protein Research, Osaka University, Suita, Osaka 565-0871 (Japan)

Dextran glucosidase from S. mutans was crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to 2.2 Å resolution. 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 P2{sub 1}2{sub 1}2{sub 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.

OSTI ID:
22360532
Journal Information:
Acta Crystallographica. Section F, Vol. 63, Issue Pt 9; Other Information: PMCID: PMC2376310; PMID: 17768352; PUBLISHER-ID: en5250; OAI: oai:pubmedcentral.nih.gov:2376310; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English