编码嗜热栖热放线菌纤维小体整合蛋白CipA单个黏连蛋白结构域的DNA片段的亚克隆：编码多肽的纯化、结晶及初步衍射分析
Subcloning of a DNA fragment encoding a single cohesin domain of the Clostridium thermocellum cellulosome-integrating protein CipA: purification, crystallization, and preliminary diffraction analysis of the encoded polypeptide.
作者信息
Béguin P, Raynaud O, Chaveroche M K, Dridi A, Alzari P M
机构信息
Unité de Physiologie Cellulaire, URA 1300 CNRS, Institut Pasteur, Paris, France.
出版信息
Protein Sci. 1996 Jun;5(6):1192-4. doi: 10.1002/pro.5560050623.
Abstract
An Escherichia coli clone encoding a single cohesin domain of the cellulosome-integrating protein CipA from Clostridium thermocellum was constructed, and the corresponding polypeptide was purified, treated with papain, and crystallized from a PEG 8000 solution. Crystals exhibit orthorhombic symmetry, space group P2(1)2(1)2(1), with cell dimensions a = 37.7 A, b = 80.7 A, c = 93.3 A, and four or eight molecules in the unit cell. The crystals diffract X-rays to beyond 2 A resolution and are suitable for further crystallographic studies.
摘要
构建了一个编码来自嗜热栖热菌的纤维小体整合蛋白CipA单个黏连蛋白结构域的大肠杆菌克隆，并纯化了相应的多肽，用木瓜蛋白酶处理后，从聚乙二醇8000溶液中结晶。晶体呈现正交对称，空间群为P2(1)2(1)2(1)，晶胞尺寸a = 37.7 Å，b = 80.7 Å，c = 93.3 Å，晶胞中有四个或八个分子。这些晶体的X射线衍射分辨率超过2 Å，适合进一步的晶体学研究。
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