Purification, crystallization and preliminary X-ray study of beta-xylosidase from Trichoderma reesei

Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):1058-60. doi: 10.1107/s0907444900008210.

Abstract

An extracellular multifunctional beta-xylosidase was purified from a culture of the fungus Trichoderma reesei. The active 95 +/- 5 kDa enzyme has been crystallized from sodium acetate buffer using PEG as a precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 67.75, b = 98.54, c = 227.25 A, and diffract beyond 2.7 A resolution. X-ray data were collected from frozen crystals on a synchrotron source.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Molecular Weight
  • Trichoderma / enzymology*
  • Xylosidases / chemistry*
  • Xylosidases / isolation & purification

Substances

  • Xylosidases
  • exo-1,4-beta-D-xylosidase