Table 1. Cryo-EM data collection, refinement and validation statistics.
CBF3core−Ndc10DBD (EMD-0095, PDB 6GYP) |
CBF3−CEN3 (EMD-0096, PDB 6GYS) |
CBF3msk (EMD-0099, PDB 6GYU) |
|
---|---|---|---|
Data collection and processing | |||
Magnification | 132,075 | 132,075 | 132,075 |
Voltage (kV) | 300 | 300 | 300 |
Electron exposure (e−/Å2) | ~28 | ~28 | ~28 |
Defocus range (μm) | 2.4-3.5 | 2.4-3.5 | 2.4-3.5 |
Pixel size (Å) | 1.06 | 1.06 | 1.06 |
Symmetry imposed | C1 | C1 | C1 |
Initial particle images (no.) | 757,433 | 987,484 | 987,484 |
Final particle images (no.) | 73,894 | 22,668 | 198,010 |
Map resolution (Å) | 3.6 | 4.4 | 3.0 |
FSC threshold | 0.143 | 0.143 | 0.143 |
Map resolution range (Å) | 3.3-4.5 | 3.7-8.3 | 2.5-3.7 |
Refinement | |||
Initial model used (PDB code) | 2QUQ,4ACO,1FQV,2HAP | 2QUQ,4ACO,1FQV,2HAP | 2QUQ,1FQV,2HAP |
Model resolution (Å) | 3.6 | 4.4 | 3.0 |
FSC threshold | 0.143 | 0.143 | 0.143 |
Model resolution range (Å) | |||
Map sharpening B factor (Å2) | -120 | -110 | -120 |
Model composition | |||
Non-hydrogen atoms | 17,811 | 38,882 | 18,157 |
Protein residues | 2,800 | 5,688 | 2,800 |
Ligands | 0 | 8 | 2 |
B factors (Å2) | |||
Protein | 174.4 | 304.1 | 148.9 |
Ligand | - | 395.4 | 181.3 |
R.m.s. deviations | 0.006 | 0.007 | 0.005 |
Bond lengths (Å) | 0.895 | 1.018 | 0.872 |
Bond angles (°) | 0.693 | 0.811 | 0.780 |
Validation | |||
MolProbity score | 1.71 | 1.77 | 1.72 |
Clashscore | 4.86 | 6.07 | 5.00 |
Poor rotamers (%) | 0.50 | 0.29 | 0.74 |
Ramachandran plot | |||
Favored (%) | 92.83 | 93.36 | 93.58 |
Allowed (%) | 7.08 | 6.48 | 6.28 |
Disallowed (%) | 0.09 | 0.16 | 0.14 |