Extended Data Table 1.
The statistics of cryo-EM structures in this study.
| TTC-pause (EMDB-33996) (PDB 7YP9) |
TTC-hairpin (EMDB-33997) (PDB 7YPA) |
TTC-release (EMDB-33998) (PDB 7YPB) |
|
|---|---|---|---|
| Data collection and processing | |||
| Magnification | 22,500 | 22,500 | 64,000 |
| Voltage (kV) | 300 | 300 | 300 |
| Electron exposure (e−/Å2) | 60.8 | 58.5 | 49.6 |
| Defocus range (μm) | −1.2 to −2.2 | −1.8 to −2.6 | −1.2 to −2.2 |
| Pixel size (Å) | 1.0 | 1.307 | 1.1 |
| Symmetry imposed | C1 | C1 | C1 |
| Initial particle images (no.) | 203,216 | 497,373 | 592,713 |
| Final particle images (no.) | 132,648 | 294,721 | 54,471 |
| Map resolution (Å) | 3.58 | 3.05 | 3.48 |
| FSC threshold | 0.143 | 0.143 | 0.143 |
| Map resolution range (Å) | 3-5 | 2.5-4.5 | 3-6 |
| Refinement | |||
| Initial model used (PDB code) | 6ALF | 6ASX | 6ASX |
| Model resolution (Å) | 3.5 | 3.0 | 3.4 |
| FSC threshold | 0.143 | 0.143 | 0.143 |
| Model resolution range (Å) | 3-5 | 2.5-4.5 | 3-6 |
| Map sharpening B factor (Å2) | −112.57 | −59.23 | −90.8 |
| Model composition | |||
| Non-hydrogen atoms | 24,548 | 26,022 | 25,626 |
| Protein residues | 3,013 | 3,129 | 3,133 |
| Ligands | 2/1 | 2/1 | 2/1 |
| B factors (Å2) | |||
| Protein | 35.89 | 43.66 | 31.81 |
| Nucleotide | 56.84 | 110.2 | 113.78 |
| Ligand | 52.73 | 63.86 | 49.7 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.003 | 0.003 | 0.002 |
| Bond angles (°) | 0.674 | 0.575 | 0.556 |
| Validation | |||
| MolProbity score | 1.52 | 1.27 | 1.23 |
| Clashscore | 5.57 | 3.02 | 2.96 |
| Poor rotamers (%) | 0.08 | 0.08 | 0.04 |
| Ramachandran plot | |||
| Favored (%) | 96.56 | 96.94 | 97.23 |
| Allowed (%) | 3.44 | 3.06 | 2.77 |
| Disallowed (%) | 0 | 0 | 0 |