Table 1.
Cryo-EM data collection, refinement and validation statistics
| Data collection and processing | Model comparison | ||
| Magnification | ×105 000 | Nonhydrogen atoms | 5990 |
| Voltage (kV) | 300 | Protein residues | 665 |
| Electron exposure e–/Å2 | 54 | B factors (Å2) | |
| Defocus range (μm) | 0.8 to 2.0 | Protein | 28–633 |
| Pixel size (Å) | 0.84 | r.m.s. deviations | |
| Symmetry imposed | C1 | Bond lengths (Å2) | 0.0060 |
| Initial particle images (no) | 539000 | Bond angles (°) | 1.3192 |
| Final particle images (no) | 149000 | Validation | |
| Map resolution (Å) | 3.6 | MolProbity score | 1.49 |
| FSC threshold | 1.43 | Clashscore | 5.24 |
| Map resolution range (Å) | 3.6 to >5.5 | Poor rotamers (%) | 0.36 |
| Refinement | Ramachandran plot | ||
| Initial model used | 1NHI | Favoured (%) | 96.66 |
| Model resolution (Å) | 3.7 | Allowed (%) | 3.44 |
| FSC threshold | 0.143 | Disallowed (%) | 0.0 |
| Map sharpening B factor (Å2) | 70 |