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Biochim Biophys Acta. 2010 Feb;1797(2):272-7. doi: 10.1016/j.bbabio.2009.11.004. Epub 2009 Nov 17.

Row-like organization of ATP synthase in intact mitochondria determined by cryo-electron tomography.

Author information

1
Electron microscopy group, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands.

Abstract

The fine structure of intact, close-to-spherical mitochondria from the alga Polytomella was visualized by dual-axis cryo-electron tomography. The supramolecular organization of dimeric ATP synthase in the cristae membranes was investigated by averaging subvolumes of tomograms and 3D details at approximately 6 nm resolution were revealed. Oligomeric ATP synthase is composed of rows of dimers at 12 nm intervals; the dimers make a slight angle along the row. In addition, the main features of monomeric ATP synthase, such as the conically shaped F(1) headpiece, central stalk and stator were revealed. This demonstrates the capability of dual-axis electron tomography to unravel details of proteins and their interactions in complete organelles.

PMID:
19925775
DOI:
10.1016/j.bbabio.2009.11.004
[Indexed for MEDLINE]
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