CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE CATALYTIC DOMAIN OF XYLANASE-A FROM PSEUDOMONAS-FLUORESCENS SUBSPECIES CELLULOSA

被引：17

作者：

PICKERSGILL, RW

JENKINS, JA

SCOTT, M

CONNERTON, I

HAZLEWOOD, GP

GILBERT, HJ

机构：

[1] INST ANIM PHYSIOL & GENET RES, DEPT BIOCHEM, CAMBRIDGE CB2 4AT, ENGLAND

[2] UNIV NEWCASTLE UPON TYNE, DEPT BIOL & NUTR SCI, NEWCASTLE UPON TYNE NE1 7RU, TYNE & WEAR, ENGLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 229卷 / 01期

关键词：

CRYSTALLIZATION; XYLANASE; PSEUDOMONAS-FLUORESCENS SUBSP CELLULOSA; X-RAY STRUCTURE;

D O I：

10.1006/jmbi.1993.1023

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 the xylan-degrading enzyme xylanase A, from Pseudomonas fluorescens subspecies cellulosa, has been expressed in Escherichia coli and crystallized. The crystals are well ordered and diffract to 1.8 AÅ using X-rays generated at the Photon Factory in Japan. The crystals are orthorhombic, space group P212121 with a = 95.7 AÅ, b = 97.1 AÅ and c = 149.8 AÅ (all ±0.2 AÅ). The similarity of the a and b cell edges, the intensity of the reflections along c* and the self rotation function results suggest a pseudo-tetragonal arrangement of molecules in the unit cell. There are probably four molecules in the asymmetric unit. © 1993 Academic Press, Inc.

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页码：246 / 248

页数：3

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