CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION ANALYSIS OF CRYSTALS OF THERMOASCUS-AURANTIACUS XYLANASE

被引：11

作者：

VISWAMITRA, MA

BHANUMOORTHY, P

RAMAKUMAR, S

MANJULA, MV

VITHAYATHIL, PJ

MURTHY, SK

NAREN, AP

机构：

[1] INDIAN INST SCI,DEPT BIOCHEM,BANGALORE 560012,KARNATAKA,INDIA

[2] INDIAN INST SCI CAMPUS,JAWAHARLAL NEHRU CTR ADV SCI RES,BANGALORE 560012,INDIA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 232卷 / 03期

关键词：

THERMOASCUS-AURANTIACUS; CRYSTALLIZATION; X-RAY CRYSTALLOGRAPHY; XYLANASE;

D O I：

10.1006/jmbi.1993.1444

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：

Crystals suitable for high resolution X-ray diffraction analysis have been grown of the 29,774-Da protein, xylanase (1,-4-beta-xylan xylanohydrolase EC 3.2.1.8) from the thermophilic fungus Thermoascus aurantiacus. This protein, an endoxylanase demonstrates the hydrolysis of β-(1-4)-d-xylose linkage in xylans and crystallizes as monoclinic pinacoids in the presence of ammonium sulphate buffered at pH 6·5, and also with neutral polyethylene glycol 6000. The crystals belong to space group P 21 and have cell dimensions, a = 41·2 Å, b = 67·76 Å, c = 51·8 Å; β = 113·2°. © 1993 Academic Press. All rights reserved.

引用

页码：987 / 988

页数：2

共 9 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].