| Electron microscope |
Krios |
| Magnification |
29,000 |
| Number of micrographs |
2055 |
| Number of particles picked from good micrographs |
162,713 |
| Number of particles used in final reconstruction |
141,549 |
| Pixel size (Å) |
0.822 |
| Defocus range (μm) |
–0.2 to –1.5 |
| Voltage (kV) |
300 |
| Electron dose (e-/Å2) |
80 |
|
Map refinement
|
|
| Model resolution (Å) |
2.2 |
| FSC threshold |
0.143 |
| Model resolution range (Å) |
2.2–20 |
| Map sharpening B-factor (Å2) |
–55.86 |
|
Refinement and model statistics
|
|
| Clashscore, all atoms |
2.23 |
|
Protein geometry
|
| MolProbity score |
1.29 |
| Rotamer outliers (%) |
0.92 |
| Cβ deviations > 0.25 Å (%) |
0.32 |
| Ramachandran (%) |
|
| - Favored |
95.79 |
| - Allowed |
4.01 |
| - Outliers |
0.2 |
| Deviations from ideal geometry |
|
| - Bonds (%) |
0.03 |
| - Angles (%) |
0.08 |
|
Nucleic acid geometry
|
| Probably wrong sugar puckers (%) |
0.84 |
| Bad backbone conformations (%) |
12.86 |
| Bad bonds (%) |
0.07 |
| Bad angles (%) |
0.08 |
