Table 1.
Cryo-EM data collection, refinement and validation statistics for nsp131-RTC, nsp132-RTC, and (nsp132-RTC)2.
| nsp131-RTC (EMDB-24431) (PDB 7RE2) | nsp132-RTC (composite) (EMDB-24430) (PDB 7RE1) | (nsp132-RTC)2 (EMDB-24432) (PDB 7RE3) | |
|---|---|---|---|
|
| |||
| Data collection and processing | |||
| Magnification | 81,000 | ||
| Voltage (kV) | 300 | ||
| Electron exposure (e–/Å2) | 66 | ||
| Defocus range (μm) | −0.8 to −2.5 | ||
| Pixel size (Å) | 1.07 | ||
| Symmetry imposed | C1 | ||
| Initial particle images (no.) | 3,750,107 | ||
| Final particle images (no.) | 85,187 | 315,120 | 35,392 |
| Map resolution (Å) | 3.2 | 2.8 | 3.3 |
| FSC threshold 0.143 | |||
| Map resolution range (Å) | 2.7–6.2 | 2.1–6.7 | 2.9–6.4 |
| Refinement | |||
| Initial models used (PDB code) | 6XEZ, 6YYT, 6ZSL | 6XEZ, 6YYT, 6ZSL | 6XEZ, 6YYT, 6ZSL |
| Model resolution (Å) | 3.2 | 2.8 | 3.3 |
| FSC threshold 0.5 | |||
| Map sharpening B factor (Å2) | −81.9 | −61.1 | −97.4 |
| Model composition | |||
| Non-hydrogen atoms | 17,096 | 21,825 | 43,154 |
| Protein residues | 1,963 | 2,553 | 5,106 |
| Nucleic acid residues (RNA) | 71 | 71 | 142 |
| Ligands | 13 | 19 | 34 |
| B factors (Å2) | |||
| Protein | 67.76 | 88.73 | 151.00 |
| Nucleic acids | 151.77 | 175.13 | 158.63 |
| Ligand | 76.87 | 77.6 | 200.51 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.005 | 0.004 | 0.004 |
| Bond angles (°) | 0.591 | 0.655 | 0.997 |
| Validation | |||
| MolProbity score | 2.11 | 2.54 | 2.60 |
| Clashscore | 8.79 | 7.84 | 10.86 |
| Poor rotamers (%) | 2.42 | 8.64 | 6.67 |
| Ramachandran plot | |||
| Favored (%) | 94.98 | 94.02 | 93.68 |
| Allowed (%) | 5.02 | 5.98 | 6.32 |
| Disallowed (%) | 0 | 0 | 0 |