Crystallization and preliminary X-ray diffraction analysis of a new xyloglucanase from Xanthomonas campestris pv. campestris

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):676-8. doi: 10.1107/S174430911301275X. Epub 2013 May 25.

Abstract

Xyloglucanases (Xghs) are important enzymes involved in xyloglucan modification and degradation. Xanthomonas campestris pv. campestris (Xcc) is a phytopathogenic bacterium which produces a large number of glycosyl hydrolases (GH), but has only one family 74 GH (Xcc-Xgh). This enzyme was overexpressed in Escherichia coli, purified and crystallized. Diffraction data sets were collected for the native enzyme and its complex with glucose to maximum resolutions of 2.0 and 2.1 Å, respectively. The data were indexed in a hexagonal crystal system with unit-cell parameters a = b = 153.4, c = 84.9 Å. As indicated by molecular-replacement solution, the crystals belonged to space group P6(1).

Keywords: GH74 family; Xanthomonas campestris pv. campestris; xyloglucanase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / analysis
  • Bacterial Proteins / chemistry*
  • Crystallization
  • Glycoside Hydrolases / analysis
  • Glycoside Hydrolases / chemistry*
  • X-Ray Diffraction
  • Xanthomonas campestris / enzymology*

Substances

  • Bacterial Proteins
  • Glycoside Hydrolases
  • xyloglucan endo(1-4)-beta-D-glucanase