Table 1 Cryo-EM data collection, refinement and validation statistics
From: Structural insights into C3 convertase activity of the classical pathway of complement
| Â | C4b2 no SP PDB 9QJ5 EMDB-53199 | C4b2 PDB 9QJ4 EMDB-53198 | C4b2b PDB 9QPY EMDB-53288 | C4b2bC3 PDB 9QK2 EMDB-53217 |
|---|---|---|---|---|
Microscope | Krios | Â | Talos Arctica | Â |
Camera | Gatan K3 Summit + GIF | Â | Gatan K2 Summit + GIF | Â |
Magnification | 105,000 | Â | 130,000 | Â |
Voltage (kV) | 300 | Â | 200 | Â |
Exposure time (s) | 2.2 | Â | 4.0/6.0 | Â |
Number of frames | 50 | Â | 40 | Â |
Electron exposure (e-/ Ã…2) | 50 | Â | 50/52 | Â |
Defocus range (µm) | −1.0 to −2.2 |  | −0.8 to −2.6 |  |
Pixel size (Ã…) | 0.836 | Â | 1.04 | Â |
Micrographs (no.) | 4662 | Â | 1700/2576 | Â |
Initial particle images (no.) | 765,438 | Â | 589,457 | Â |
Final particles images (no.) | 111,565 | 31,587 | 17,073 | 177,801 |
Map Resolution (Ã…) 0.143 FSC threshold | 3.5 | 4.0 | 4.2 | 3.5 |
Refinement | ||||
Model Resolution (Ã…) 0.5 FSC threshold | 3.6 | 4.0 | 4.2 | 3.6 |
Map sharpening B factor (Å2) | −100 | −100 | −120 | −100 |
Model composition | ||||
 Non-hydrogen atoms | 12,950 | 15,254 | 16,917 | 29,917 |
 Protein residues | 1657 | 1948 | 2154 | 3793 |
 Ligands | NAG: 3, MG: 1 | NAG: 3, MG: 1 | NAG: 7, MG: 1 | NAG: 8, MG: 1 |
R.m.s. deviations | ||||
 Bond lengths (Å) | 0.003 | 0.004 | 0.003 | 0.003 |
 Bond angles (o) | 0.688 | 0.837 | 0.671 | 0.566 |
Validation | ||||
 MolProbity score | 1.70 | 1.86 | 1.89 | 1.58 |
 Clashscore | 8.48 | 11.32 | 14.88 | 4.95 |
 Rotamer outliers (%) | 0.42 | 0.54 | 0.05 | 1.13 |
Ramachandran plot | ||||
 Favored (%) | 96.40 | 95.80 | 96.71 | 95.93 |
 Allowed (%) | 3.60 | 4.20 | 3.24 | 4.07 |
 Outliers (%) | 0.00 | 0.00 | 0.05 | 0.00 |
