Table 2.
Cryo-EM structures data collection, refinement and validation statistics (continued)
| Name of structure | A/H7N9 K289A/C489R revertant Apo-dimer with promoter | A/H7N9 self-stalled termination product complex with bound CTD |
|---|---|---|
| PDB ID | PDB ID 8POH | PDB ID 8R3K |
| EMDB ID | EMD-17792 | EMD-18871 |
| Data collection and processing | ||
| Microscope | ThermoFisher Glacios | ThermoFisher Glacios |
| Voltage (kV) | 200 | 200 |
| Camera | Falcon IV/Selectris X | Falcon IV/Selectris X |
| Magnification | 130k | 130k |
| Nominal defocus range (μm) | −0.8/−2.0 | −0.8/−2.0 |
| Electron exposure (e–/Å2) | 40 | 40 |
| Number of fractions processed (no.) | 24 | 24 |
| Pixel size (Å) | 0.907 | 0.878 |
| Micrographs (no.) | 5092 | 3509 |
| Refinement | ||
| Particles per class (no.) | 278761 | 29072 |
| Map resolution (Å), 0.143 FSC | 3.26 | 3.43 |
| Model resolution (Å), 0.5 FSC | 3.38 | 3.40 |
| Map sharpening B factor (Å2) | −140 | −55 |
| Map versus model cross-correlation (CCmask) | 0.7456 | 0.8472 |
| Model composition | ||
| Non-hydrogen atoms | 20729 | 14287 |
| Protein residues | 2479 | 1718 |
| Nucleotide residues | 38 | 41 |
| Water | - | - |
| Ligands | 1 Mg | 2 Mg, PPi |
| B factors (Å2) | ||
| Protein | 105.84 | 55.88 |
| Nucleotide | 123.86 | 61.19 |
| Ligand | 33.48 | 44.02 |
| Water | - | - |
| R.M.S. deviations | ||
| Bond lengths (Å) | 0.003 | 0.003 |
| Bond angles (°) | 0.562 | 0.507 |
| Validation | ||
| MolProbity score | 1.84 | 1.44 |
| All-atom clash score | 6.79 | 6.44 |
| Poor rotamers (%) | 2.37 | 0.07 |
| Ramachandran plot | ||
| Favoured (%) | 96.91 | 97.59 |
| Allowed (%) | 3.09 | 2.41 |
| Outliers (%) | 0.0 | 0.0 |