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Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe)

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  • Bioinformatics Research Centre (BiRC)
  • Interdisciplinary Nanoscience Center
  • Department of Molecular Biology
  • Department of Molecular Biology
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.
Original languageEnglish
JournalF E B S Letters
Volume356
Issue2-3
Pages (from-to)165-8
Number of pages3
ISSN0014-5793
Publication statusPublished - 1994

    Research areas

  • 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

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