Table 1 CryoEM data collection, structure determination and model statistics.
From: Structural insight into mitochondrial β-barrel outer membrane protein biogenesis
SAM in lipid nanodiscs | SAM in detergent | |||||
|---|---|---|---|---|---|---|
Data collection | ||||||
Nominal magnification | ×130,000 | ×130,000 | ||||
Voltage (kV) | 300 | 300 | ||||
Exposure time (s/frame) | 0.2 | 0.2 | ||||
Number of frames | 50 | 50 | ||||
Total dose (e-/Å2) | 69 | 69 | ||||
Defocus range (μm) | −0.8 to −3.0 | −0.8 to −3.0 | ||||
Pixel size (Å) | 1.06 | 1.06 | ||||
Image processing | ||||||
Micrographs selected | 11,347 | 10,831 | ||||
Dimer 1 | Monomer from Dimer 1 | Dimer 2 | Dimer 3 | Monomer | ||
Initial particle images (no.) | 3,951,406 | 174,217 | – | 112,106 | 380,304 | 514,800 |
Final particle images (no.) | 179,509 | 117,339 | 335,670 | 60,472 | 122,361 | 138,575 |
Symmetry imposed | C1 | C2 | C1 | C2 | C2 | C1 |
FSC threshold | 0.143 | 0.143 | 0.143 | 0.143 | 0.143 | 0.143 |
Final map resolution (Å) | 3.4 | 3.2 | 3.0 | 3.6 | 3.9 | 3.7 |
Atomic model | ||||||
Number of protein residues | 1037 | 2190 | 1087 | 2192 | 1326 | 887 |
Validation | ||||||
Most favored (%) | 87.51 | 87.21 | 93.8 | 83.49 | 81.6 | 83.93 |
Allowed (%) | 12.49 | 12.7 | 6.2 | 16.42 | 18.4 | 16.07 |
Disallowed (%) | 0 | 0.09 | 0 | 0.09 | 0 | 0 |
Rotamer outliers (%) | 5.42 | 6.92 | 5.79 | 1.06 | 1.14 | 0 |
r.m.s.d Bond lengths (Å) | 0.003 | 0.005 | 0.008 | 0.008 | 0.005 | 0.007 |
r.m.s.d Bond angles (°) | 0.651 | 0.812 | 0.876 | 0.922 | 0.79 | 0.887 |
Clashscore | 8.96 | 7.98 | 3.66 | 10.08 | 13.92 | 9.69 |
Map CC (main chain) | 0.79 | 0.8 | 0.83 | 0.81 | 0.79 | 0.81 |
Map CC (side chain) | 0.77 | 0.78 | 0.81 | 0.8 | 0.78 | 0.79 |
Deposition ID | ||||||
EMDB | EMD-21913 | EMD-21915 | EMD-21918 | EMD-21916 | EMD-21917 | EMD-21914 |
PDB | 6WUH | 6WUL | 6WUT | 6WUM | 6WUN | 6WUJ |
