English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  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.

Item is

Files

show Files

Locators

show

Creators

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

Content

show
hide
Free keywords: electron cryotomography
 Abstract: 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.

Details

show
hide
Language(s): eng - English
 Dates: 2014-06-19
 Publication Status: Published online
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 695746
DOI: 10.1038/ncomms5129
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 5 Sequence Number: 4129 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723