Table 1. Cryo-EM data collection, refinement and validation statistics.
| Uncleavable closed (EMDB-11203, PDB 6ZGE) | Cleaved closed (EMDB-11207, PDB 6ZGI) | Intermediate (EMDB-11206, PDB 6ZGH) | Cleaved open (EMDB-11205, PDB 6ZGG) | Bat virus (EMDB-11204, PDB 6ZGF) | |
|---|---|---|---|---|---|
| Data collection and processing | |||||
| Voltage (kV) | 300 | 300 | 300 | 300 | 300 |
| Electron exposure (e–/Å2) | 33.6 | 54.4 | 54.4 | 54.4 | 54.4 |
| Defocus range (μm) | -1.5 to -3.0 | -1.5 to -3.0 | -1.5 to -3.0 | -1.5 to -3.0 | -1.5 to -3.0 |
| Pixel size (Å) | 1.09 | 1.08 | 1.08 | 1.08 | 1.08 |
| Symmetry imposed | C3 | C3 | C1 | C1 | C3 |
| Final particle images (no.) | 95 K | 95 K | 107 K | 73 K | 62 K |
| Map resolution (Å) FSC threshold = 0.143 | 2.6 | 2.9 | 6.8 | 3.8 | 3.1 |
| Map resolution range (Å) | 2.4–3.2 | 2.8–3.6 | 6–10 | 3.5–7.5 | 3.0–3.8 |
| Refinement | |||||
| Initial model used (PDB code) | 6VXX | - | - | - | - |
| Model resolution (Å) FSC threshold = 0.5 | 2.7 | 3.0 | 8.2 | 4.1 | 3.2 |
| Map sharpening B factor (Å2) | -109.8 | -91.2 | -207.0 | -61.7 | -88.2 |
| Model composition | |||||
| Non-hydrogen atoms | 26991 | 26901 | 23735 | 25111 | 26169 |
| Protein residues | 3294 | 3294 | 3032 | 3207 | 3180 |
| Ligands | 81 | 78 | - | - | 93 |
| B factors (Å2) | |||||
| Protein | 35.1 | 47.8 | - | - | 37.13 |
| Ligand | 83.0 | 77.5 | - | - | 52.15 |
| R.m.s. deviations | |||||
| Bond lengths (Å) | 0.009 | 0.006 | 0.003 | 0.003 | 0.007 |
| Bond angles (°) | 0.902 | 0.753 | 0.855 | 0.863 | 1.130 |
| Validation | |||||
| MolProbity score | 1.33 | 1.21 | 1.69 | 1.79 | 1.70 |
| Clashscore | 2.20 | 1.64 | 3.20 | 3.79 | 5.16 |
| Poor rotamers (%) | 0.73 | 0.73 | 0.90 | 0.98 | 0.75 |
| Ramachandran plot | |||||
| Favored (%) | 95.22 | 95.68 | 88.94 | 87.13 | 93.57 |
| Allowed (%) | 4.69 | 4.23 | 10.75 | 12.36 | 6.43 |
| Disallowed (%) | 0.09 | 0.09 | 0.30 | 0.50 | 0.00 |