CRYSTALLIZATION AND PRELIMINARY DIFFRACTION ANALYSIS OF THE CATALYTIC DOMAIN OF XYLANASE-Z FROM CLOSTRIDIUM-THERMOCELLUM

被引：10

作者：

SOUCHON, H

SPINELLI, S

BEGUIN, P

ALZARI, PM

机构：

[1] INST PASTEUR,CNRS,UNITE IMMUNOL STRUCT 359,25 RUE DR ROUX,F-75724 PARIS 15,FRANCE

[2] INST PASTEUR,CNRS,UNITE PHYSIOL CELLULAIRE 1300,F-75724 PARIS 15,FRANCE

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1994年 / 235卷 / 04期

关键词：

CRYSTALLIZATION; XYLANASE; CLOSTRIDIUM-THERMOCELLUM; X-RAY CRYSTALLOGRAPHY;

D O I：

10.1006/jmbi.1994.1089

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The catalytic domain of a thermostable xylanase from Clostridium thermocellum has been expressed in Escherichia coli and crystallized from a polyethylene glycol 2000 solution by the hanging drop method. Crystals belong to the triclinic space group P1 with cell dimensions a = 46.8 Å, b = 50.8 Å, c = 70.3 Å, α = 100.7°, β = 83.8°, γ = 101.6°, and two molecules in the unit cell. These crystals diffract X-rays to at least 1.8 Å resolution and are suitable for high-resolution X-ray analysis. © 1994 Academic Press Limited.

引用

页码：1348 / 1350

页数：3

共 16 条

[1] CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION ANALYSIS OF THE CATALYTIC DOMAIN OF CEX, AN EXO-BETA-1,4-GLUCANASE AND BETA-1,4-XYLANASE FROM THE BACTERIUM CELLULOMONAS-FIMI [J].