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  Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-TU, from Escherichia coli

Kabsch, W., Gast, W. H., Schulz, G. E., & Lebermann, R. (1977). Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-TU, from Escherichia coli. Journal of Molecular Biology (London), 117(4), 999-1012. doi:10.1016/S0022-2836(77)80009-0.

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Datensatz-Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-B11C-E Versions-Permalink: http://hdl.handle.net/21.11116/0000-0001-2BF2-E
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JMolBiol_117_1977_999.pdf (beliebiger Volltext), 3MB
 
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 Urheber:
Kabsch, Wolfgang1, 2, Autor              
Gast, W. H., Autor
Schulz, Georg E.1, Autor              
Lebermann, Reuben, Autor
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, escidoc:1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, escidoc:1497700              

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 Zusammenfassung: The low resolution structure of a trypsin-modified form of elongation factor EF-Tu from Escherichia coli has been determined by X-ray crystallographic methods. The crystals belong to space group P212121 with two molecules in the asymmetric unit. The phase determination was based on three isomorphous heavy-atom derivatives. The quality of the resulting electron density map at 6 Å was sufficient to identify the molecules. The two molecules in the asymmetric unit are related by a non-crystallographic 2-fold rotation. A molecular model was derived by averaging the electron density of the two molecules at equivalent points. Its overall dimensions are 75 Å × 50 Å × 35 Å. The molecule consists of a compact globular head of dimensions 45 Å × 40 Å × 40 Å and a curled tail of diameter 25 Å and length 55 Å. There is a second connection between head and tail, probably an α-helix, such that the molecule forms a ring. The large groove in the centre could accommodate a RNA double helix. The head has a high α-helical content whereas the tail seems to be helix-free. A molecular weight of 43,000 was derived from the electron density map indicating that no major part of the molecule is missing. Possible interactions between EF-Tu and transfer RNA are discussed.

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Sprache(n): eng - Englisch
 Datum: 1977-07-281977-09-202005-05-021977-12-25
 Publikationsstatus: Im Druck publiziert
 Seiten: 14
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
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Titel: Journal of Molecular Biology (London)
  Andere : J Mol Biol
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: London : Academic Press
Seiten: - Band / Heft: 117 (4) Artikelnummer: - Start- / Endseite: 999 - 1012 Identifikator: ISSN: 0022-2836
CoNE: http://pubman.mpdl.mpg.de/cone/journals/resource/954922646042