Table 1.
Cryo-EM data collection, refinement and validation statistics
| Csy-AcrIF4 (EMD-22582, PDB 7JZW) | Csy-AcrIF7 (EMD-22583, PDB 7JZX) | Csy-AcrIF14 (EMD-22585, PDB 7JZZ) | |
|---|---|---|---|
| Data collection and processing | |||
| Magnification | 81 000 | 81 000 | 81 000 |
| Voltage (kV) | 300 | 300 | 300 |
| Electron exposure (e–/Å2) | 54 | 54 | 54 |
| Defocus range (μm) | 1.5–2.5 | 1.5–2.5 | 1.5–2.5 |
| Pixel size (Å) | 1.05 | 1.05 | 1.05 |
| Symmetry imposed | C1 | C1 | C1 |
| Initial particle images (no.) | 1 765,062 | 1 627 883 | 1 217 862 |
| Final particle images (no.) | 766 782 | 502 177 | 226 089 |
| Map resolution (Å) | 3.2 | 3.4 | 3.2 |
| FSC threshold | 0.143 | 0.143 | 0.143 |
| Map resolution range (Å) | 3–4.2 | 3.2–4.4 | 3–4.2 |
| Refinement | |||
| Initial model used | PDB 6NE0 | PDB 7JZW | PDB 7JZW |
| Model resolution (Å) | 3.2 | 3.4 | 3.2 |
| FSC threshold | 0.5 | 0.5 | 0.5 |
| Model resolution range (Å) | 3.2–50 | 3.4–50 | 3.2–50 |
| Map sharpening B factor (Å2) | –112 | –129 | –86 |
| Model composition | |||
| Non-hydrogen atoms | 24 266 | 23 948 | 24 767 |
| Protein residues | 2986 | 2954 | 3092 |
| Nucleotides | 61 | 61 | 61 |
| Ligands | 0 | 0 | 0 |
| B factors (Å2) | |||
| Protein | 28.49 | 65.26 | 48.40 |
| Nucleotide | 58.01 | 75.10 | 81.07 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.010 | 0.009 | 0.010 |
| Bond angles (°) | 0.977 | 0.921 | 0.980 |
| Validation | |||
| MolProbity score | 1.75 | 1.73 | 1.76 |
| Clashscore | 5.65 | 5.33 | 5.72 |
| Poor rotamers (%) | 0.13 | 0.40 | 0.00 |
| Ramachandran plot | |||
| Favored (%) | 93.00 | 92.99 | 93.07 |
| Allowed (%) | 7.00 | 7.01 | 6.93 |
| Disallowed (%) | 0.00 | 0.00 | 0.00 |