Table 1 Cryo-EM data collection, refinement and validation statistics
Di-heptamer | Long | Short | Folded | Unfolded | |
---|---|---|---|---|---|
EMDB ID | EMD-33188 | EMD-32043 | EMD-32041 | EMD-34136 | EMD-34137 |
PDB ID | – | 7VNN | 7VNJ | 7YVQ | 7YVS |
Data collection and processing | |||||
Magnification | 81,000 | ||||
Voltage (kV) | 300 | ||||
Electron exposure (e-/Å2) | 50 | ||||
Defocus range (μm) | −0.8 to −2.0 | ||||
Pixel size (Å) | 0.88 | ||||
Symmetry imposed | C1 | ||||
Initial particle images (no.) | 2,608,418 | ||||
Final particle images (no.) | 102,116 | 83,061 | 167,398 | 24,981 | 100,912 |
Map resolution (Å) | 3.19 | 2.64 | 2.56 | 3.18 | 2.80 |
FSC threshold | 0.143 | 0.143 | 0.143 | 0.143 | 0.143 |
Map sharpening B factor (Å2) | −67.1 | −32.3 | −36.4 | −56.1 | −70.9 |
Refinement | |||||
Model resolution (Å) | – | 3.2 | 2.8 | 3.4 | 3.0 |
FSC threshold | – | 0.5 | 0.5 | 0.5 | 0.5 |
Model composition | |||||
Non-hydrogen atoms | – | 38,823 | 30,661 | 30,742 | 30,593 |
Protein residues | – | 4863 | 3856 | 3874 | 3856 |
Ligands | – | 21 | 21 | 21 | 21 |
B factors (Å2) | |||||
Protein | – | 61.64 | 93.72 | 90.02 | 78.04 |
Ligand | – | 45.36 | 77.75 | 73.97 | 63.43 |
R.m.s deviations | |||||
Bond lengths (Å) | – | 0.004 | 0.004 | 0.005 | 0.005 |
Bond angles (Å) | – | 0.949 | 0.956 | 0.977 | 0.990 |
Validation | |||||
MolProbity score | – | 1.74 | 1.65 | 1.76 | 1.68 |
Clashscore | – | 6.31 | 5.58 | 6.34 | 6.12 |
Poor rotamers (%) | – | 0.37 | 0.40 | 0.75 | 0.98 |
Ramachandran plot | |||||
Favored (%) | – | 94.27 | 95.01 | 93.78 | 95.09 |
Allowed (%) | – | 5.73 | 4.99 | 6.22 | 4.91 |
Disallowed (%) | – | 0.00 | 0.00 | 0.00 | 0.00 |