Crystallization and preliminary crystallographic analysis of dextranase from Streptococcus mutans

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Dec 1;67(Pt 12):1542-4. doi: 10.1107/S1744309111038425. Epub 2011 Nov 25.

Abstract

Streptococcus mutans dextranase hydrolyzes the internal α-1,6-linkages of dextran and belongs to glycoside hydrolase family 66. An N- and C-terminal deletion mutant of S. mutans dextranase was crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 1.6 Å and belonged to space group P2(1), with unit-cell parameters a = 53.2, b = 89.7, c = 63.3 Å, β = 102.3°. Assuming that the asymmetric unit of the crystal contained one molecule, the Matthews coefficient was calculated to be 4.07 Å(3) Da(-1); assuming the presence of two molecules in the asymmetric unit it was calculated to be 2.03 Å(3) Da(-1).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Dextranase / chemistry*
  • Streptococcus mutans / enzymology*

Substances

  • Dextranase