Table 1.
Cryo-EM data collection, refinement and validation statistics
U1-OC (EMDB-15009, PDB 7ZXE) | U1-OC, local map (EMDB-15007, PDB-7ZX8) | U1-CC (EMDB-15006, PDB-7ZX7) | U5-CC (EMDB-14997, (PDB-7ZWD) | U5-CC, local map (EMDB-14996, PDB- 7ZWC) | |
---|---|---|---|---|---|
Data collection and processing | |||||
Magnification | ×81,000 | ×81,000 | |||
Voltage (kV) | 300 | 300 | |||
Electron exposure (e–/Å2) | 54.45 | 51.93 | |||
Defocus range (μm) | −0.5 to −3.0 | −0.5 to −2.5 | |||
Pixel size (Å) | 1.05 | 1.05 | |||
Micrographs collected | 16,854 | 4,842 | |||
Initial particle images (no.) | 5,181,947 | 1,299,523 | |||
Final particle images (no.) | 137,246 | 137,246 | 47,293 | 85,787 | 85,787 |
Map resolution (Å) | 3.0 | 3.5 | 3.4 | 3.0 | 3.2 |
FSC threshold | 0.143 | 0.143 | 0.143 | 0.143 | 0.143 |
Map resolution range (Å) | 2.8–5.2 | 3.4–6.0 | 3.0–7.0 | 2.75–5.25 | 3.0–5.0 |
Refinement | |||||
Initial model used (PDB code) | 7NVU | 7NVU | 7NVS | 7NVS | 7NVS |
Map sharpening B factor (Å2) | −10 | −10 | −5 | −10 | −10 |
Model composition | |||||
DNA | 126 | 93 | 132 | 132 | 83 |
Protein residues | 5,842 | 1,500 | 5,789 | 5,789 | 1,500 |
Ligands | 11 | 2 | 12 | 12 | 2 |
B factors (Å2) | |||||
DNA | 276.52 | 174.43 | 318.34 | 248.19 | 95.70 |
Protein residues | 133.43 | 186.65 | 215.69 | 124.47 | 109.50 |
Ligands | 192.93 | 155.55 | 237.49 | 194.42 | 82.54 |
R.m.s. deviations | |||||
Bond lengths (Å) | 0.005 | 0.003 | 0.004 | 0.007 | 0.003 |
Bond angles (°) | 0.755 | 0.606 | 0.509 | 0.658 | 0.524 |
Validation | |||||
MolProbity score | 1.78 | 1.68 | 1.69 | 1.63 | 1.67 |
Clashscore | 9.52 | 8.46 | 9.85 | 7.55 | 7.63 |
Poor rotamers (%) | 0.16 | 0.00 | 0.00 | 0.00 | 0.00 |
CaBLAM outliers | 1.93 | 1.73 | 1.63 | 1.91 | 2.07 |
Cβ outliers | 0.00 | 0.00 | 0.00 | 0.00 | 0.00 |
Ramachandran plot | |||||
Favored (%) | 95.91 | 96.61 | 97.03 | 96.68 | 96.27 |
Allowed (%) | 4.09 | 3.39 | 2.97 | 3.32 | 3.73 |
Disallowed (%) | 0.00 | 0.00 | 0.00 | 0.00 | 0.00 |