Expression, purification, crystallization and preliminary X-ray analysis of the iota-carrageenase from Alteromonas fortis

Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):766-8. doi: 10.1107/s0907444900004844.

Abstract

This is the first crystallization report of a glycoside hydrolase which belongs to family 82. A recombinant form of His-tagged iota-carrageenase from Alteromonas fortis was expressed, purified and crystallized. Crystals were obtained by the vapour-diffusion method using polyethylene glycol (M(W) = 6000) as a precipitant. They belong to space group P2(1), with unit-cell parameters a = 56. 75, b = 91.04, c = 125.01 A, beta = 93.41 degrees. The unit cell contains two molecules in the asymmetric unit related by a non-crystallographic twofold axis. Crystals diffracted to 2.0 A resolution on a synchrotron beamline.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alteromonas / enzymology*
  • Alteromonas / genetics
  • Bacterial Proteins*
  • Carrageenan / metabolism*
  • Crystallization
  • Crystallography, X-Ray
  • Gene Expression Regulation, Bacterial
  • Genes, Bacterial
  • Glycoside Hydrolases / biosynthesis
  • Glycoside Hydrolases / genetics*
  • Glycoside Hydrolases / isolation & purification*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / isolation & purification

Substances

  • Bacterial Proteins
  • Recombinant Proteins
  • Carrageenan
  • Glycoside Hydrolases
  • kappa-carrageenase protein, Alteromonadaceae