Table 1 Cryo-EM data collection, refinement and validation statistics for mAb1 and mAb2 structures.
mAb1 full complex | mAb1 | mAb1 | mAb2 full complex | |
|---|---|---|---|---|
2 trimers:3 mAbs | Masked | 2 trimers:2 mAbs | 2 trimers:3 mAbs | |
(EMDB-23293) | (−) | (EMDB-23295) | (EMDB-23296) | |
(PDB 7LEX) | (−) | (PDB 7LEZ) | (PDB 7LF0) | |
Data collection and processing | ||||
Magnification | 130,000 | 130,000 | 130,000 | 130,000 |
Voltage (kV) | 300 | 300 | 300 | 300 |
Electron exposure (e–/Å2) | 45.46 | 45.46 | 45.46 | 44.32 |
Defocus range (μm) | −1.0 to −1.8 | −1.0 to −1.8 | −1.0 to −1.8 | −1.2 to −2.0 |
Pixel size (Å) | 1.04 | 1.04 | 1.04 | 1.04 |
Symmetry imposed | C3 | C3 | C1 | C3 |
Initial particle images (no.) | 94,796 | 94,796 | 94,796 | 52,550 |
Final particle images (no.) | 37,385 | 77,986 | 16,810 | 52,550 |
Map resolution (Å) | 3.6 | 3.4 | 4.1 | 3.7 |
FSC threshold | 0.143 | 0.143 | 0.143 | 0.143 |
Refinement | ||||
Initial model used (PDB code) | 6V7C | 6V7C | 6V7C | 6V7C |
Model resolution (Å) | 3.6 | 3.5 | 4.3 | 3.8 |
FSC threshold | 0.5 | 0.5 | 0.5 | |
Map sharpening B factor (Å2) | 106.7 | 134.6 | 77.9 | 109.7 |
Model composition | ||||
Non-hydrogen atoms | 25,662 | 25,662 | 21,628 | 25,797 |
Protein residues | 4554 | 4554 | 3654 | 4542 |
Ligands | 0 | 0 | 0 | 0 |
B factors (Å2) | ||||
Protein | 76.2 | 118.8 | 224.2 | 56.6 |
Ligand | — | — | — | — |
R.m.s. deviations | ||||
Bond lengths (Å) | 0.009 | 0.011 | 0.007 | 0.010 |
Bond angles (°) | 1.00 | 1.09 | 1.14 | 1.07 |
Validation | ||||
MolProbity score | 1.89 | 1.96 | 2.14 | 2.03 |
Clashscore | 6.42 | 6.9 | 11.4 | 7.5 |
Poor rotamers (%) | 0.31 | 0.78 | 0.65 | 1.09 |
Ramachandran plot | ||||
Favored (%) | 90.4 | 89.3 | 89.2 | 87.8 |
Allowed (%) | 8.7 | 9.8 | 10.1 | 11.4 |
Disallowed (%) | 0.89 | 0.89 | 0.66 | 0.80 |
