Crystallization and preliminary X-ray analysis of an exotype alginate lyase Atu3025 from Agrobacterium tumefaciens strain C58, a member of polysaccharide lyase family 15

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 May 1;62(Pt 5):486-8. doi: 10.1107/S1744309106014333. Epub 2006 Apr 28.

Abstract

Almost all alginate lyases depolymerize alginate in an endolytical fashion via a beta-elimination reaction. The alginate lyase Atu3025 from Agrobacterium tumefaciens strain C58, consisting of 776 amino-acid residues, is a novel exotype alginate lyase classified into polysaccharide lyase family 15. The enzyme was crystallized at 293 K by sitting-drop vapour diffusion with polyethylene glycol 4000 as a precipitant. Preliminary X-ray analysis showed that the Atu3025 crystal belonged to space group P2(1) and diffracted to 2.8 angstroms resolution, with unit-cell parameters a = 107.7, b = 108.3, c = 149.5 angstroms, beta = 91.5 degrees.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agrobacterium tumefaciens / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Polysaccharide-Lyases / chemistry*

Substances

  • Polysaccharide-Lyases
  • poly(beta-D-mannuronate) lyase