| Literature DB >> 19925775 |
Natalya V Dudkina1, Gert T Oostergetel, Dagmar Lewejohann, Hans-Peter Braun, Egbert J Boekema.
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. 2009 Elsevier B.V. All rights reserved.Mesh：
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Year: 2009 PMID： 19925775 DOI： 10.1016/j.bbabio.2009.11.004
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002