Table 2 Cryo-EM data collection, refinement and validation statistics for S-UK:ACE2 complex and nAb cocktails
From: Effect of SARS-CoV-2 B.1.1.7 mutations on spike protein structure and function
Data collection and processing | ||
Magnification | ×81,000 | ×81,000 |
Voltage (kV) | 300 | 300 |
Electron exposure (e–/Å2) | 50 | 50 |
Defocus range (μm) | 0.8–2.6 | 0.8–2.6 |
Pixel size (Å) | 1.1 | 1.1 |
Symmetry imposed | C1 | C3 |
Initial particle images (no.) | 2,328,218 | 772,531 |
Final particle images (no.) | 463,191 | 79,794 |
Map resolution (Å) | 3.3 | 4.0 |
FSC threshold | 0.143 | 0.143 |
Refinement | ||
Initial model used (PDB code) | ||
Model resolution (Å) | 3.1 | 4.2 |
FSC threshold | 0.143 | 0.143 |
Map sharpening B factor (Å2) | −102.9 | −118.1 |
Model composition | ||
Nonhydrogen atoms | 39,571 | 34,992 |
Protein residues | 4,836 | 4,362 |
Ligands | 84 | 75 |
B factors (Å2) | ||
Protein | 10.66 | 0.17 |
Ligand | 55.15 | 37.41 |
R.m.s. deviations | ||
Bond lengths (Å) | 0.005 | 0.002 |
Bond angles (°) | 0.659 | 0.518 |
Validation | ||
MolProbity score | 1.95 | 1.92 |
Clashscore | 8.42 | 10.12 |
Poor rotamers (%) | 0.00 | 0.16 |
Ramachandran plot | ||
Favored (%) | 91.84 | 94.23 |
Allowed (%) | 7.99 | 5.56 |
Disallowed (%) | 0.17 | 0.21 |
