Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 272-277 |
| Seitenumfang | 6 |
| Fachzeitschrift | Biochimica et Biophysica Acta - Bioenergetics |
| Jahrgang | 1797 |
| Ausgabenummer | 2 |
| Publikationsstatus | Veröffentlicht - 17 Nov. 2009 |
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 ∼ 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 F1 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.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biophysik
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Zellbiologie
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in: Biochimica et Biophysica Acta - Bioenergetics, Jahrgang 1797, Nr. 2, 17.11.2009, S. 272-277.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Row-like organization of ATP synthase in intact mitochondria determined by cryo-electron tomography
AU - Dudkina, Natalya V.
AU - Oostergetel, Gert T.
AU - Lewejohann, Dagmar
AU - Braun, Hans Peter
AU - Boekema, Egbert J.
N1 - Funding information: N.V.D. is supported by a VENI grant from the Netherlands Organization for Scientific Research NWO. We thank D.N. Mastronarde (University of Colorado), R. Kou?il and W. Keegstra for discussion.
PY - 2009/11/17
Y1 - 2009/11/17
N2 - 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 ∼ 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 F1 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.
AB - 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 ∼ 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 F1 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.
KW - ATP synthase
KW - Electron tomography
KW - Mitochondria
KW - Polytomella
UR - http://www.scopus.com/inward/record.url?scp=73249153664&partnerID=8YFLogxK
U2 - 10.1016/j.bbabio.2009.11.004
DO - 10.1016/j.bbabio.2009.11.004
M3 - Article
C2 - 19925775
AN - SCOPUS:73249153664
VL - 1797
SP - 272
EP - 277
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
SN - 0005-2728
IS - 2
ER -