@article{43529f10f9c311dd8f9a000ea68e967b,
title = "Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe)",
abstract = "Elongation factor Tu (EF-Tu) is the most abundant protein in prokaryotic cells. Its general function in protein biosynthesis is well established. It is a member of the large family of G-proteins, all of which bind guanosine phosphates (GDP or GTP) as cofactors. In its active GTP bound state EF-Tu binds aminoacylated tRNA (aa-tRNA) forming the ternary complex EF-Tu:GTP:aa-tRNA. The ternary complex interacts with the ribosome where the anticodon on tRNA recognises a codon on mRNA, GTPase activity is induced and inactive EF-Tu:GDP is released. Here we report the successful crystallization of a ternary complex of Thermus aquaticus EF-Tu:GDPNP and yeast Phe-tRNA(Phe) after its purification by HPLC.",
keywords = "Chromatography, Gel, Chromatography, High Pressure Liquid, Crystallization, Crystallography, X-Ray, Electrophoresis, Polyacrylamide Gel, Guanosine Triphosphate, Guanylyl Imidodiphosphate, Peptide Elongation Factor Tu, RNA, Transfer, Phe, Saccharomyces cerevisiae, Thermus",
author = "P Nissen and L Reshetnikova and G Siboska and G Polekhina and S Thirup and M Kjeldgaard and Clark, {B F} and J Nyborg",
year = "1994",
language = "English",
volume = "356",
pages = "165--8",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "John Wiley & Sons Inc.",
number = "2-3",
}