Table 1. Cryo-EM data collection, refinement and validation statistics.
M. musculus apoferritin (EMDB-10205) (PDB 6SHT) | |
---|---|
Data collection and processing | |
Magnification | 150,000X |
Voltage (kV) | 200 |
Electron exposure (e–/Å2) | 28 |
Defocus range (μm) | -0.8 to -1.6 |
Pixel size (Å) | 0.96 |
Symmetry imposed | O |
Initial particle images (no.) | 211,177 |
Final particle images (no.) | 95,733 |
Map resolution (Å) | 2.73 |
FSC threshold | 0.143 |
Map resolution range (Å) | 2.73–3.21 (Relion) |
2.10–3.60 (ResMap) | |
Refinement | |
Initial model used (PDB code) | 3wnw |
Model resolution (Å) | 2.76 |
FSC threshold | FSC = 0.143 |
Model resolution range (Å) | 2.76–2.99a |
Map sharpening B factor (Å2) | -95.1618 |
Model composition | |
Non-hydrogen atoms | 1474 |
Protein residues | 173 |
Ligands | 74 |
B factors (Å2) | |
Protein | 34.8 |
Ligand | 36.6 |
R.m.s. deviations | |
Bond lengths (Å) | 0.015 |
Bond angles (°) | 1.524 |
Validation | |
Clashscore | 5.96 |
Poor rotamers (%) | 2.5 |
Ramachandran plot | |
Favored (%) | 98.9 |
Allowed (%) | 0.5 |
Disallowed (%) | 0.6 |
aresolution range includes resolution values reported at FSC = 0.143 against half-maps, unprocessed, unmasked map and the final processed masked map (S4 Fig).