嗜热水生栖热袍菌Ffh和FtsY的NG结构域的GMPPCP复合物的结晶
Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY.
作者信息
Shepotinovskaya Irina V, Focia Pamela J, Freymann Douglas M
机构信息
Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Medical School, 303 East Chicago Avenue, Chicago, IL 60611, USA.
出版信息
Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1834-7. doi: 10.1107/s0907444903016573. Epub 2003 Sep 19.
Abstract
The GTPases Ffh and FtsY are components of the prokaryotic signal recognition particle protein-targeting pathway. The two proteins interact in a GTP-dependent manner, forming a complex that can be stabilized by use of the non-hydrolyzable GTP analog GMPPCP. Crystals of the complex of the NG GTPase domains of the two proteins have been obtained from ammonium sulfate solutions. Crystals grow with several different morphologies, predominately as poorly diffracting plates and needle clusters, but occasionally as well diffracting rods. It has been demonstrated that all forms of the crystals observed contain an intact complex. Diffraction data to 2.0 A resolution have been measured.
摘要
GTP酶Ffh和FtsY是原核生物信号识别颗粒蛋白质靶向途径的组成部分。这两种蛋白质以GTP依赖的方式相互作用，形成一个复合物，该复合物可通过使用不可水解的GTP类似物GMPPCP来稳定。两种蛋白质的NG GTP酶结构域复合物的晶体已从硫酸铵溶液中获得。晶体以几种不同的形态生长，主要是衍射能力差的片状和针状簇，但偶尔也会出现衍射能力良好的棒状。已证明观察到的所有晶体形式都包含完整的复合物。已测量了分辨率为2.0埃的衍射数据。
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