Extended Data Table 1.
Cryo-EM data collection, refinement, and validation statistics
| Human S-0PA1 membrane-proximal conformation (EMDB-26977) (PDB 8CT1) | Human S-OPA1 membrane-distal conformation (EMDB-26984) (PDB 8CT9) | |
|---|---|---|
| Data collection and processing | ||
| Microscope | FEI Titan Krios | |
| Camera | Gatan K3 Summit | |
| Magnification | 105,000x | |
| Voltage (kV) | 300 | |
| Electron exposure (e−/Å2) | 65 | |
| Defocus (μm) | −0.5 to −1.2 | |
| Pixel size (Å) | 0.833 | |
| Symmetry imposed | helical | |
| Micrographs (no.) | 12,237 | |
| Initial particle images (no.) | 623,000 | |
| Symmetry expanded particle images (no.) | 4,248,873 | |
| Final particle images (no.) | 139,018 | 96,152 |
| Map resolution (Å) | 4.8 | 6.8 |
| FSC threshold | 0.143 | 0.143 |
| Map resolution range (Å) | 3.7 to >10.0 | 5.6 to >10.0 |
| Refinement | ||
| Initial model used (PDB code) | de novo - G domain (6JTG) | de novo - G domain (6JTG) |
| Model resolution (Å) | 4.7 | 7.8 |
| FSC threshold | 0.143 | 0.143 |
| Map sharpening B factor (Å2) | −198.51 | −200.00 |
| Model composition | ||
| Non hydrogen atoms | 193,290 | 198,307 |
| Protein residues | 23,732 | 23,732 |
| Lipids | 91 | |
| B factors (Å2) - min | ||
| Protein | 97.85 | 202.86 |
| Ligands | 390.35 | |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.001 | 0.006 |
| Bond angles (Å) | 0.309 | 0.570 |
| Validation | ||
| MolProbity score | 1.19 | 1.17 |
| Clashscore | 4.06 | 3.82 |
| Poor rotamers (%) | 0.0 | 0.0 |
| Ramachandran plot | ||
| Favored (%) | 99.57 | 98.60 |
| Allowed (%) | 0.43 | 1.40 |
| Disallowed (%) | 0.0 | 0.0 |