F1 Fo ATP synthase dimer at 4.1 Å resolution. Subunit a, blue; c-ring, yellow; ASA 6, brick; other subunits, cyan; detergent micelle, grey.
c-ring rotor, yellow; subunit a, dark blue; subunit ASA 6, brick; α and β subunits of catalytic F1 head, green; central stalk subunits, light blue; oligomycin-sensitivity conferring protein (OSCP), …
(A) Electron micrograph of detergent-solubilised ATP synthase dimers. Scale bar, 500 Å; (B) Fourier shell correlation (FSC) curve and local resolution for the 1.6 MDa dimer indicate 4.1 Å overall …
Strictly conserved aArg239, light blue; conserved charged and polar residues, pink; small residues aAla246, aGly247 and aAla292 at the point where the lumenal channel passes between H5 and H6, green;…
(A) Side view with fitted subunit a, trans-membrane helices of ASA 6 and c-ring. (B) Subunit a and ASA 6 seen from the c-ring. (C) subunit a, c-ring and ASA 6 seen from the matrix. Subunit a, blue; c…
Subunit a, blue; ASA 6, brick; c10-ring, yellow. The strictly conserved aArg239 in its well-defined map density is highlighted (blue ellipse).
(A) Lumenal channel seen from the crista lumen. (B) Matrix channel seen from the matrix. (C) Side view of both channels seen from the c-ring, with outer c-ring helices in transparent yellow. Lumenal …
(A) In the lumenal channel, protons (red arrow) pass via the local proton reservoir of aGlu172, aHis248, aHis252 and aGlu288 (dashed red ellipse) through the H5/H6 helix hairpin at the small …
(A) Lumenal channel passing through the H5/H6 helix hairpin at aAla246, aGly247 (H5) and aAla292 (H6) (green). (B) aArg239 is located halfway between the lumenal channel on the left and the matrix …
(A) Lipid density modelled as two phosphatidyl glycerol molecules (grey) between subunit a (blue) and ASA 6 (brick); (B) detergent density modelled as dodecyl maltoside and hydrophobic alkyl chain …
(A) Lumenal channel; (B) matrix channel. Sidechains in stick representation are coloured as: subunit a, blue; subunit c-ring, yellow; ASA 6, brick. Channels are shown as potential surfaces (red, …
(A) Proton reservoir formed by aGlu172, aHis248, aHis252, aGlu288 (dashed red ellipse) in the lumenal channel; (B) Interaction of aAsn243 (H5) and aGln295 (H6) stabilises the H5/H6 hairpin. The …
(A) Residues in a-subunit helices H4, H5 and H6, which are implicated in diseases are highlighted in orange. (B) Trp189 and Tyr299/Thr193 that act as wedges between H4 and H5.
The c-ring (yellow) and the membrane-intrinsic four-helix bundle of subunit a (blue) drawn to scale as seen from the matrix. Protons (red) pass from the crista lumen below the projection plane …
showing the two c-rings (yellow), subunits a (blue) and ASA 6 (brick). The remaining eight ASA subunits in the peripheral stalks, the central stalks and catalytic F1 heads are shown in transparent …
Sidechains in stick representation are coloured as: subunit a, blue; c-ring, yellow; ASA 6, brick; lipids, grey. Channels are shown as potential surfaces (red, negative; blue, positive; grey, …
Sidechains in stick representation are coloured as: subunit a, blue; c-ring, yellow; ASA 6, brick. Channels are shown as potential surfaces (red, negative; blue, positive; grey, neutral).
Data collection | |
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Electron Microscope | JEOL JEM-3200FSC |
Camera | K2 Summit |
Voltage | 300 kV |
Energy filter slit width | 20 eV |
Nominal Magnification | 30,000 x |
Calibrated physical pixel size | 1.12 Å |
Pixel size after mag. distortion corr. | 1.105 Å |
Total exposure | 82.5 e-/Å2 |
Exposure rate | 11.5 e-/(pixel x s) |
Number of frames | 45 |
Defocus range | −0.4 to −5 μm (95% between -0.9 and -2.5 µm) |
Image Processing | |
Motion correction software | Unblur/MotionCor2 (with mag. distortion corr.) |
CTF estimation software | CTFFind4, Gctf (for per-particle CTF) |
Particle selection software | e2boxer (EMAN2) |
Micrographs used | 9,518 |
Particles selected | 117,281 |
3D map classification and refinement software | Relion2 |
Particles contributing to final map | 90,142 |
Applied symmetry | C2 |
Global resolution (FSC = 0.143) | 3.68 Å |
Applied B-factor | -125 Å |
Model Building | |
Modeling software | Coot |
Refinement software | Phenix (phenix.real_space_refine) |
Number of residues built | 1,039 |
RMS (bonds) | 0.01 Å |
RMS (angles) | 1.09° |
Ramachandran outliers | 0.0% |
Ramachandran favoured | 94.88% |
Rotamer outliers | 0.27% |
Clashscore | 7.5 |
EMRinger score | 1.42 |