Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY.
Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY.
复制标题
栖热菌 Ffh 和 FtsY NG 结构域的 GMPPCP 复合物的结晶。
DOI：
10.1107/s0907444903016573
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发表时间：
2003
期刊：
影响因子：
--
通讯作者：
Freymann,DouglasM
中科院分区：
文献类型：
--
作者：
Shepotinovskaya,IrinaV;Focia,PamelaJ;Freymann,DouglasM
GTP酶Ffh和FtsY是原核信号识别颗粒蛋白靶向途径的组分。这两种蛋白质以GTP依赖性方式相互作用，形成复合物，该复合物可以通过使用不可水解的GTP类似物GMPPCP来稳定。已从硫酸铵溶液中获得两种蛋白质的NG GT3结构域的复合物的晶体。晶体生长有几种不同的形态，主要是衍射差的板和针簇，但偶尔也有衍射棒。已经证明，观察到的所有形式的晶体都含有完整的复合物。测量了分辨率为2.0 μ m的衍射数据。
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 Å resolution have been measured.