CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE LEPIDOPTERAN-SPECIFIC INSECTICIDAL CRYSTAL PROTEIN CRYLA(A)

被引：6

作者：

BORISOVA, S

GROCHULSKI, P

VANFAASSEN, H

PUSZTAICAREY, M

MASSON, L

CYGLER, M

机构：

[1] NATL RES COUNCIL CANADA, BIOTECHNOL RES INST, MONTREAL H4P 2R2, PQ, CANADA

[2] NATL RES COUNCIL CANADA, INST BIOL SCI, OTTAWA K1A 0R6, ON, CANADA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1994年 / 243卷 / 03期

关键词：

PROTEIN CRYSTALLIZATION; INSECTICIDAL CRYSTAL PROTEIN; DELTA-ENDOTOXIN; BACILLUS THURINGIENSIS TOXIN;

D O I：

10.1006/jmbi.1994.1678

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：

A trypsin-activated CrylA(a) protein from Bacillus thuringiensis has been purified and crystallized. Crystals belong to orthorhombic space group P2(1)2(1)2(1), with cell dimensions a = 53.3, b = 111.3 and c = 154.7 Angstrom. The crystals diffract to at least 2.2 Angstrom resolution and are suitable for X-ray structural analysis. They contain a single molecule in the asymmetric unit.

引用

页码：530 / 532

页数：3

共 24 条

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