鳞翅目特异性杀虫晶体蛋白CrylA(a)的结晶及初步X射线衍射研究。

Crystallization and preliminary X-ray diffraction studies of the lepidopteran-specific insecticidal crystal protein CrylA(a).

作者信息

Borisova S, Grochulski P, van Faassen H, Pusztai-Carey M, Masson L, Cygler M

机构信息

Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec.

出版信息

J Mol Biol. 1994 Oct 28;243(3):530-2. doi: 10.1006/jmbi.1994.1678.

DOI:10.1006/jmbi.1994.1678

PMID:7966278

Abstract

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 A. The crystals diffract to at least 2.2 angstrum resolution and are suitable for X-ray structural analysis. They contain a single molecule in the asymmetric unit.

摘要

一种来自苏云金芽孢杆菌的经胰蛋白酶激活的CrylA(a)蛋白已被纯化并结晶。晶体属于正交晶系空间群P2(1)2(1)2(1)，晶胞参数a = 53.3、b = 111.3和c = 154.7 Å。这些晶体的衍射分辨率至少为2.2埃，适合进行X射线结构分析。它们在不对称单元中包含一个单分子。