Table 1 Summary of single-particle data collection, 3D reconstruction, and model refinement.
From: CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae
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 |
