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  Visualizing active membrane protein complexes by electron cryotomography

Gold, V. A. M., Ieva, R., Walter, A., Pfanner, N., van der Laan, M., & Kühlbrandt, W. (2014). Visualizing active membrane protein complexes by electron cryotomography. Nature Communications, 5: 4129. doi:10.1038/ncomms5129.

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Genre: Zeitschriftenartikel

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 Urheber:
Gold, Vicky A. M.1, Autor           
Ieva, Raffaele, Autor
Walter, Andreas1, Autor           
Pfanner, Nikolaus, Autor
van der Laan, Martin, Autor
Kühlbrandt, Werner1, Autor                 
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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Schlagwörter: electron cryotomography
 Zusammenfassung: Unravelling the structural organization of membrane protein machines in their active state and native lipid environment is a major challenge in modern cell biology research. Here we develop the STAMP (Specifically TArgeted Membrane nanoParticle) technique as a strategy to localize protein complexes in situ by electron cryotomography (cryo-ET). STAMP selects active membrane protein complexes and marks them with quantum dots. Taking advantage of new electron detector technology that is currently revolutionizing cryotomography in terms of achievable resolution, this approach enables us to visualize the three-dimensional distribution and organization of protein import sites in mitochondria. We show that import sites cluster together in the vicinity of crista membranes, and we reveal unique details of the mitochondrial protein import machinery in action. STAMP can be used as a tool for site-specific labelling of a multitude of membrane proteins by cryo-ET in the future.

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Sprache(n): eng - English
 Datum: 2014-06-19
 Publikationsstatus: Online veröffentlicht
 Seiten: 9
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 695746
DOI: 10.1038/ncomms5129
 Art des Abschluß: -

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Titel: Nature Communications
  Kurztitel : Nat. Commun.
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: London : Nature Publishing Group
Seiten: - Band / Heft: 5 Artikelnummer: 4129 Start- / Endseite: - Identifikator: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723