Table 1.
Cryo-EM data collection, refinement, and validation statistics for p300(BRPHΔAILZ)-NCP complexes
| Sample | Complex I |
Complex II |
Complex III |
Complex IV |
|---|---|---|---|---|
| (EMD-32373, PDB 7W9V) | (EMD-32374) | (EMD-32375) | (EMD-32376) | |
| Data collection | ||||
| Electron microscope | Krios G3i | |||
| Camera | K3 | |||
| Magnification | 81,000× | |||
| Pixel size (Å/pix) | 1.07 | |||
| Defocus range (μm) | −1.2 to −2.3 | |||
| Exposure time (second) | 10 | |||
| Total dose (e/Å2) | 1st dataset: 55.975, 2nd dataset: 56.149 | |||
| Movie frames (no.) | 40 | |||
| Total micrographs (no.) | 14,102 | |||
| Reconstruction | ||||
| Software | Relion 3.1 | |||
| Particles for 2D classification | 8,811,235 | |||
| Particles for 3D classification | 2,778,145 | |||
| Particles in the final map (no.) | 25,884 | 145,147 | 25,208 | 227,652 |
| Symmetry | C1 | C1 | C1 | C1 |
| Final resolution (Å) | 3.95 | 3.38 | 3.95 | 3.29 |
| FSC threshold | 0.143 | 0.143 | 0.143 | 0.143 |
| Map sharpening B factor (Å2) | −28.8 | −30.0 | −35.5 | −35.9 |
| Model building | ||||
| Software | Coot | |||
| Refinement | ||||
| Software | Phenix | |||
| Model composition | ||||
| Protein | 1,302 | |||
| Nucleotide | 290 | |||
| Validation | ||||
| MolProbity score | 1.47 | |||
| Clash score | 8.50 | |||
| R.m.s. deviations | ||||
| Bond lengths (Å) | 0.006 | |||
| Bond angles (˚) | 0.948 | |||
| Ramachandran plot | ||||
| Favored (%) | 97.97 | |||
| Allowed (%) | 2.03 | |||
| Outliers (%) | 0 | |||