Expression, purification and preliminary X-ray diffraction analysis of the catalytic module of a beta-agarase from the flavobacterium Zobellia galactanivorans

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Apr 1;66(Pt 4):413-7. doi: 10.1107/S174430911000429X. Epub 2010 Mar 31.

Abstract

Marine bacteria secrete specific glycoside hydrolases such as agarases to access polysaccharides from algal cell walls as a carbon and energy source. In an attempt to identify agarases with variable degradation patterns, a novel family GH16 beta-agarase from the marine bacterium Zobellia galactanivorans was expressed, purified and crystallized. The purified enzyme crystallized in two distinct forms that were grown by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant. Hexagonal crystals belonging to space group P3(1)21 diffracted to 2.2 A resolution, whereas orthorhombic crystals belonging to space group P2(1)2(1)2(1) diffracted to 1.5 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biocatalysis*
  • Crystallography, X-Ray
  • Flavobacteriaceae / enzymology*
  • Gene Expression
  • Glycoside Hydrolases / chemistry*
  • Molecular Sequence Data
  • Sequence Alignment

Substances

  • Glycoside Hydrolases
  • agarase