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单头和双头驱动蛋白的结晶及初步X射线分析

Crystallization and preliminary X-ray analysis of the single-headed and double-headed motor protein kinesin.

作者信息

Kozielski F, Schönbrunn E, Sack S, Müller J, Brady S T, Mandelkow E

机构信息

Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany.

出版信息

J Struct Biol. 1997 Jun;119(1):28-34. doi: 10.1006/jsbi.1997.3872.

DOI:10.1006/jsbi.1997.3872
PMID:9216086
Abstract

Crystals of the single-headed and double-headed kinesin motor domains of Rattus norvegicus have been grown by vapor diffusion using ammonium sulfate as the precipitant. Both crystal systems belong to the orthorhombic space group P2(1)2(1)2(1). Double-headed kinesin crystallized with unit cell constants of a = 72.2 A, b = 91.9 A, and c = 141.7 A, and so far the best crystals diffracted to a maximum resolution of 2.7 A. Using ammonium sulfate single-headed kinesin crystallized in two different crystal forms with cell constants of a = 73.1 A, b = 73.2 A, c = 84.0 A and a = 73.4 A, b = 74.1 A, c = 74.7 A, respectively. They were found to diffract to 2.1 A resolution. Crystals of monomeric kinesin were also obtained with lithium sulfate as precipitant. They have cell constants of a = 71.6 A, b = 73.7 A, and c = 74.1 A and diffract up to 1.7 A resolution.

摘要

利用硫酸铵作为沉淀剂,通过气相扩散法培养出了褐家鼠单头和双头驱动蛋白运动结构域的晶体。这两种晶体系统都属于正交空间群P2(1)2(1)2(1)。双头驱动蛋白结晶时的晶胞常数为a = 72.2 Å、b = 91.9 Å、c = 141.7 Å,到目前为止,最好的晶体衍射分辨率达到了2.7 Å。使用硫酸铵时,单头驱动蛋白以两种不同的晶体形式结晶,晶胞常数分别为a = 73.1 Å、b = 73.2 Å、c = 84.0 Å和a = 73.4 Å、b = 74.1 Å、c = 74.7 Å。发现它们的衍射分辨率为2.1 Å。还以硫酸锂作为沉淀剂获得了单体驱动蛋白的晶体。它们的晶胞常数为a = 71.6 Å、b = 73.7 Å、c = 74.1 Å,衍射分辨率高达1.7 Å。

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