Table 1.
Summary of single-particle data collection, 3D reconstruction, and model refinement.
| Imaging parameters and 3D reconstruction | |
| Acceleration voltage (kV) | 300 |
| Magnification (×) | 81,000 |
| Pixel size (Å) | 1.104 |
| Frame rate (s−1) | 0.092 |
| Exposure time (s) | 3.7 |
| Total exposure (e−/Å) | 60 |
| Particles | |
| Micrographs used for selection | 2,510 |
| Defocus range (µm) | −0.5 to −3.5 |
| Windowed | 252,319 |
| In final 3D reconstruction | 100,543 |
| Resolution | |
| “Gold-standard” at FSC 0.5 (Å) | 3.0 Å |
| “Gold-standard” at FSC 0.143 (Å) | 2.7 Å |
| Map-sharpening B factor (Å2) | −69 |
| Model refinement | |
| Resolution in phenix.real_space_refine (Å) | 3.0 |
| Model-to-map fit (CC_mask) | 0.745 |
| Number of atoms/residues/molecules | |
| NCS restrained chains | 14 |
| Protein atoms, residues (per chain) | 43,736, 412 |
| Ramachandran angles (%) | |
| Favored | 92.21 |
| Allowed | 7.79 |
| Outliers | 0 |
| r.m.s. deviations | |
| Bond lengths (Å) | 0.006 |
| Bond angles (°) | 0.847 |
| Molprobity | |
| Score | 2.81 |
| Clashscore | 10.53 |
| Rotamer outliers (%) | 10.91 |
| EMRinger score | 3.13 |