Crystallization and preliminary X-ray analysis of a novel unsaturated glucuronyl hydrolase from Bacillus sp. GL1

Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):946-9. doi: 10.1107/s0907444903005912. Epub 2003 Apr 25.

Abstract

Unsaturated glucuronyl hydrolase from Bacillus sp. GL1 catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides produced by the reactions of polysaccharide lyases such as gellan, xanthan, hyaluronate and chondroitin lyases. The enzyme was crystallized at 293 K from a droplet containing 56% MPD, 0.1 M NaCl, 0.1 M glycine-NaOH pH 8.2 and 0.1 M dithiothreitol using the vapour-diffusion method. The crystals were hexagonal and belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 102.8, c = 223.4 A. Diffraction data to 2.4 A were collected from a single crystal.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus / enzymology*
  • Bacillus / genetics
  • Carbohydrate Sequence
  • Crystallization
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Glycoside Hydrolases / chemistry*
  • Molecular Sequence Data
  • Oligosaccharides / metabolism
  • Recombinant Proteins / chemistry
  • X-Ray Diffraction

Substances

  • Oligosaccharides
  • Recombinant Proteins
  • Glycoside Hydrolases
  • unsaturated glucuronyl hydrolase