Table 1 Cryo-EM data collection, refinement and validation statistics.
#1 Candida albicans γ-TuSC (EMD-11835) (PDB-7ANZ) | |||
---|---|---|---|
Data collection and processing | Dataset 1 | Dataset 2 | |
Magnification | 81,000 | 81,000 | |
Voltage (kV) | 300 | 300 | |
Electron exposure (e–/Å2) | 40 | 40 | |
Defocus range (μm) | −2 to −3 | −2 to −3 | |
Pixel size (Å) | 1.07 | 1.07 | |
Initial particle images (no.) | 309,744 | 1,502,064 | |
Final particle images (no.) | 45,351 | 228,975 | |
Merged set of particles | 274,326 | – | |
Map resolution (Å) | 3.6 | – | |
FSC threshold | 0.143 | – | |
Model resolution range (Å) | 3.3-4.7 | – | |
Refinement | |||
Initial model used (PDB code) | Homology models derived from human GCP4 (3RIP) and γ-tubulin (1Z5W) | – | |
Model resolution (Å) | 3.6 | 4.2 | – |
FSC threshold | 0.143 | 0.5 | – |
Model resolution range (Å) | 3.5-4.3 | – | |
Map sharpening B factor (Å2) | −60.0 | – | |
Model composition | – | ||
Non-hydrogen atoms | 16,759 | – | |
Protein residues | 2041 | – | |
Ligands | 0 | – | |
B factors (Å2) | – | ||
Protein | 5.71/82.31/35.50 | – | |
Ligand | −/−/− | – | |
R.m.s. deviations | – | ||
Bond lengths (Å) | 0.003 | – | |
Bond angles (°) | 0.786 | – | |
Validation | – | ||
MolProbity score | 1.66 | – | |
Clashscore | 4.57 | – | |
Poor rotamers (%) | 0.31 | – | |
Ramachandran plot | – | ||
Favored (%) | 93.36 | – | |
Allowed (%) | 6.49 | – | |
Disallowed (%) | 0.15 | – |