Expression, purification, crystallization and preliminary x-ray analysis of the kappa-carrageenase from Pseudoalteromonas carrageenovora

G Michel; T Barbeyron; D Flament; T Vernet; B Kloareg; O Dideberg

doi:10.1107/s0907444998018526

Expression, purification, crystallization and preliminary x-ray analysis of the kappa-carrageenase from Pseudoalteromonas carrageenovora

Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):918-20. doi: 10.1107/s0907444998018526.

Authors

G Michel¹, T Barbeyron, D Flament, T Vernet, B Kloareg, O Dideberg

Affiliation

¹ Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS/CEA, 41 Avenue des Martyrs, 38027 Grenoble CEDEX 1, France.

PMID: 10089334
DOI: 10.1107/s0907444998018526

Abstract

A recombinant form of His-tagged kappa-carrageenase from Pseudoalteromonas carrageenovora has been expressed, purified and crystallized. Crystals have been obtained by the vapour-diffusion method using polyethylene glycol (Mr = 4000) as a precipitant. These crystals belong to the space group P212121, with unit-cell parameters a = 58.2, b = 62.8, c = 77.9 A, and diffract to 2.2 A resolution on a rotating-anode X-ray source.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Bacterial Proteins / isolation & purification
Crystallization
Escherichia coli / genetics
Glycoside Hydrolases / chemistry*
Glycoside Hydrolases / genetics
Glycoside Hydrolases / isolation & purification
Gram-Negative Aerobic Bacteria / enzymology*
Gram-Negative Aerobic Bacteria / genetics
Recombinant Proteins / biosynthesis
Recombinant Proteins / chemistry
Recombinant Proteins / isolation & purification
X-Ray Diffraction

Substances

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