Table 2. Cryo-EM data collection and refinement statistics for 30S•RNAP structures.
| non-rotated | rotated | ΔS1 | |
|---|---|---|---|
| PDB code | 6AWB | 6AWC | 6AWD |
| EMDB code | EMD-7014 | EMD-7015 | EMD-7016 |
| Data collection | |||
| EM equipment | FEI Titan Krios | FEI Titan Krios | FEI Talos Arctica |
| Voltage (kV) | 300 | 300 | 200 |
| Detector | K-2 | K-2 | K-2 |
| Pixel size (Å) | 0.82 | 0.82 | 0.94 |
| Electron dose (e-/Å2) | 40 | 40 | 40 |
| Defocus range (μm) | −0.8 to −3.0 | −0.8 to −3.0 | −0.8 to −3.0 |
| Reconstruction | |||
| Software | Frealign v9.11 | Frealign v9.11 | Frealign v9.11 |
| Number of particles used | 15,012 | 10,090 | 21123 |
| Final resolution (Å) | 6.7 | 7.9 | 8.1 |
| Map-sharpening B factor (Å2) | −198 | −205 | −200 |
| Model composition | |||
| Non-hydrogen atoms | 75316 | 75169 | 76452 |
| Protein residues | 5743 | 5726 | 5573 |
| RNA bases | 1443 | 1443 | 1539 |
| Refinement | |||
| Software | RSRef and Phenix | RSRef and Phenix | RSRef and Phenix |
| Correlation Coeff (%; Phenix) | 75.9 | 76.7 | 78.3 |
| R-factor (RSRef) | 0.250 | 0.251 | 0.257 |
| Validation (proteins) | |||
| MolProbity score | 2.70 | 2.60 | 2.67 |
| Clash score, all atoms | 20.25 | 18.90 | 20.47 |
| Ramachandran-plot statistics (%) | |||
| Favored (overall) | 80.0 | 81.9 | 79.6 |
| Allowed (overall) | 16.2 | 14.6 | 16.3 |
| Outlier (overall) | 3.8 | 3.5 | 4.1 |
| R.m.s. deviations | |||
| Bond length (Å) | 0.005 | 0.004 | 0.004 |
| Bond angle (˚) | 1.097 | 1.111 | 1.027 |
| Validation (RNA) | |||
| Correct sugar puckers (%) | 99.9 | 99.9 | 99.9 |
| Good backbone conformation (%) | 88.2 | 88.6 | 88.2 |