Purification, crystallization and preliminary X-ray analysis of a thermostable glycoside hydrolase family 43 beta-xylosidase from Geobacillus thermoleovorans IT-08

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1;63(Pt 11):932-5. doi: 10.1107/S1744309107046015. Epub 2007 Oct 24.

Abstract

The main enzymes involved in xylan-backbone hydrolysis are endo-1,4-beta-xylanase and beta-xylosidase. beta-Xylosidase converts the xylo-oligosaccharides produced by endo-1,4-beta-xylanase into xylose monomers. The beta-xylosidase from the thermophilic Geobacillus thermoleovorans IT-08, a member of glycoside hydrolase family 43, was crystallized at room temperature using the hanging-drop vapour-diffusion method. Two crystal forms were observed. Bipyramid-shaped crystals belonging to space group P4(3)2(1)2, with unit-cell parameters a = b = 62.53, c = 277.4 A diffracted to 1.55 A resolution. The rectangular crystals belonged to space group P2(1), with unit-cell parameters a = 57.94, b = 142.1, c = 153.9 A, beta = 90.5 degrees , and diffracted to 1.80 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillaceae / enzymology
  • Crystallization
  • Crystallography, X-Ray
  • Endo-1,4-beta Xylanases / chemistry*
  • Endo-1,4-beta Xylanases / isolation & purification
  • Enzyme Stability

Substances

  • Endo-1,4-beta Xylanases