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

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Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe). / Nissen, P; Reshetnikova, L; Siboska, G; Polekhina, G; Thirup, S; Kjeldgaard, M; Clark, B F; Nyborg, J.

In: F E B S Letters, Vol. 356, No. 2-3, 1994, p. 165-8.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Nissen, P, Reshetnikova, L, Siboska, G, Polekhina, G, Thirup, S, Kjeldgaard, M, Clark, BF & Nyborg, J 1994, 'Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe)', F E B S Letters, vol. 356, no. 2-3, pp. 165-8.

APA

Nissen, P., Reshetnikova, L., Siboska, G., Polekhina, G., Thirup, S., Kjeldgaard, M., Clark, B. F., & Nyborg, J. (1994). Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe). F E B S Letters, 356(2-3), 165-8.

CBE

Nissen P, Reshetnikova L, Siboska G, Polekhina G, Thirup S, Kjeldgaard M, Clark BF, Nyborg J. 1994. Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe). F E B S Letters. 356(2-3):165-8.

MLA

Vancouver

Author

Nissen, P ; Reshetnikova, L ; Siboska, G ; Polekhina, G ; Thirup, S ; Kjeldgaard, M ; Clark, B F ; Nyborg, J. / Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe). In: F E B S Letters. 1994 ; Vol. 356, No. 2-3. pp. 165-8.

Bibtex

@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 = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd.",
number = "2-3",

}

RIS

TY - JOUR

T1 - Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe)

AU - Nissen, P

AU - Reshetnikova, L

AU - Siboska, G

AU - Polekhina, G

AU - Thirup, S

AU - Kjeldgaard, M

AU - Clark, B F

AU - Nyborg, J

PY - 1994

Y1 - 1994

N2 - 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.

AB - 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.

KW - Chromatography, Gel

KW - Chromatography, High Pressure Liquid

KW - Crystallization

KW - Crystallography, X-Ray

KW - Electrophoresis, Polyacrylamide Gel

KW - Guanosine Triphosphate

KW - Guanylyl Imidodiphosphate

KW - Peptide Elongation Factor Tu

KW - RNA, Transfer, Phe

KW - Saccharomyces cerevisiae

KW - Thermus

M3 - Journal article

C2 - 7805830

VL - 356

SP - 165

EP - 168

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 2-3

ER -