Table 1:
Cryo-EM data collection, refinement and validation statistics
| Dip1–Arp2/3–actin (EMD-21502, PDB 6W17) |
Inactive Arp2/3 complex (EMD-21503, PDB 6W18) | |
|---|---|---|
| Data collection and processing | ||
| Magnification | x92,000 | x120,000 |
| Voltage (kV) | 200 | 200 |
| Electron exposure (e–/Å2) | 36.35 | 44.34 |
| Defocus range (μm) | −1.00 – −1.75 | −0.70 – −1.30 |
| Pixel size (Å) | 1.12 | 0.8757 |
| Symmetry imposed | C1 | C1 |
| Initial particle images (no.) | 3,500,000 | 3,336,981 |
| Final particle images (no.) | 110,433 | 112,170 |
| Map resolution (Å) | 3.9 | 4.2 |
| FSC threshold | 0.143 | 0.143 |
| Map resolution range (Å) | 3.5 – 5.5 | 3.9 – 6.0 |
| Refinement | ||
| Initial models used | PDB 3DWL, PDB 3J8I | PDB 3DWL |
| Model resolution (Å) | 3.92 | 4.45 |
| FSC threshold | 0.5 | 0.5 |
| Model resolution range (Å) | 2.3 – 4.0 | 3.7 – 4.5 |
| Map sharpening B factor (Å2) | −45.12 | −116.22 |
| Model composition | ||
| Non-hydrogen atoms | 27,399 | 12,727 |
| Protein residues | 3,483 | 1,854 |
| Ligands | 6 Mg2+, 2 ATP, 4 ADP, 5 Phalloidin | Mg2+, 2 ATP |
| B factors (Å2) | ||
| Protein | 102.53 | 51.05 |
| Ligand | 92.30 | 82.27 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.004 | 0.004 |
| Bond angles (°) | 0.967 | 0.983 |
| Validation | ||
| MolProbity score | 1.65 | 1.42 |
| Clashscore | 5.63 | 4.67 |
| EMRinger score | 1.39 | 1.29 |
| Poor rotamers (%) | 0.00 | 0.00 |
| Ramachandran plot | ||
| Favored (%) | 95.00 | 96.96 |
| Allowed (%) | 5.00 | 3.04 |
| Disallowed (%) | 0.00 | 0.00 |
| CaBLAM outliers (%) | 4.2 | 3.8 |