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

被引：25

作者：

Michel, G

Flament, D

Barbeyron, T

Vernet, T

Kloareg, B

Dideberg, O

机构：

[1] CEA, CNRS, Inst Biol Struct Jean Pierre Ebel, Lab Cristallog Macromol, F-38027 Grenoble 1, France

[2] Stn Biol Roscoff, CNRS, UMR 1931, F-29682 Roscoff, France

[3] Stn Biol Roscoff, Lab Goemar, F-29682 Roscoff, France

[4] CEA, CNRS, Inst Biol Struct Jean Pierre Ebel, Lab Ingn Macromol, F-38027 Grenoble 1, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2000年 / 56卷

关键词：

D O I：

10.1107/S0907444900004844

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom, 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 Angstrom resolution on a synchrotron beamline.

引用

页码：766 / 768

页数：3

共 12 条

[1] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].