Extended Data Table 1 |.
Cryo-EM data collection, refinement and validation statistics
| WaaL-WaB10 (Und-PP bound) (EMD-26054) (PDB-7TPG) |
Waal-WaB10 (apo) (EMD-26057) (PDB-7TPJ) |
|
|---|---|---|
| Data collection and processing | ||
| Magnification | 130,000 | 13,000 |
| Voltage (kV) | 300 | 300 |
| Electron exposure (e-/Å2) | 70 | 70 |
| Exposure time (s) | 2.5 | 2.5 |
| Dose rate (e-/pixel/s) | 16 | 16 |
| Nominal defocus range (μm) | 1–2 | 1–2 |
| Defocus range (μm) | 0.8–1.2 | 0.8–1.2 |
| Pixel size (Å) | 1.061 | 1.061 |
| Symmetry imposed | C1 | C1 |
| Number of micrographs | 2,378 | 2,378 |
| Initial particle imagers (no.) | 844,438 | 844,438 |
| Final particle images (no.) | 39,844 | 30,514 |
| Map resolution (Å) | 3.23 | 3.46 |
| FSC threshold | 0.143 | 0.143 |
| Sphericity of 3DFSC | 0.944 | 0.944 |
| Refinement | ||
| Map sharpening B factor (Å2) | −24.07 | −12.22 |
| Reside range | 5–407 (CmWaal) 2–105 and 5–123 (Fab) |
|
| Model composition | ||
| Non-hydrogen atoms | 4778 | 4759 |
| Protein residues | 626 | 626 |
| Ligands | 1 | 0 |
| B factors (Å2) | ||
| Protein | 43.04 | 35.95 |
| Ligand | 61.05 | ---- |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.002 | 0.004 |
| Bond angles (°) | 0.621 | 0.700 |
| Validation | ||
| MolProbity score | 1.63 | 1.83 |
| Clashscore | 7.19 | 9.09 |
| Poor rotamers (%) | 0.20 | 0.00 |
| EM-Ringer Score | 2.45 | 1.60 |
| Ramachandran plot | ||
| Favored (%) | 96.45 | 95.00 |
| Allowed (%) | 3.55 | 5.00 |
| Disallowed | 0.00 | 0.00 |