Crystallization and preliminary X-ray crystallographic study on a xyloglucan-specific exo-beta-glycosidase, oligoxyloglucan reducing-end specific cellobiohydrolase

Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1838-9. doi: 10.1107/s0907444903017128. Epub 2003 Sep 19.

Abstract

A novel xyloglucan-specific exo-beta-glycosidase, oligoxyloglucan reducing-end specific cellobiohydrolase (OXG-RCBH), recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. OXG-RCBH was crystallized by the hanging-drop vapour-diffusion method with polyethylene glycol 3000 and polyethylene glycol 400 as precipitants. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 61.0, b = 146.9, c = 211.9 A. The crystals diffract to a resolution of 2.2 A and are suitable for X-ray structure analysis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cellulose 1,4-beta-Cellobiosidase / chemistry*
  • Cellulose 1,4-beta-Cellobiosidase / metabolism
  • Crystallization / methods
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Glycoside Hydrolases / chemistry*
  • Glycoside Hydrolases / metabolism
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism

Substances

  • Recombinant Proteins
  • Glycoside Hydrolases
  • oligoxyloglucan hydrolase
  • Cellulose 1,4-beta-Cellobiosidase