Table 1. Cryo-EM data collection, refinement and validation statistics.
| Data Collection and processing | |||
|---|---|---|---|
| Microscope | Titan krios, (UCSF) | ||
| Camera | K3 | ||
| Magnification | 60,010 | ||
| Voltage (kV) | 300 kV | ||
| Electron exposure (e-/Å2) | 86.4 | ||
| Defocus range (µm) | −0.5 to −2.0 | ||
| Pixel size (Å) | 0.8332 | ||
| Software | SerialEM | ||
| Reconstruction | CI* Peripheral Arm | CI* Membrane Arm | CI* Composite Map |
| Number of particles | 34,407 | 34,407 | The CI* Peripheral Arm and Membrane Arm Maps were combined in Phenix to generate this composite map |
| Accuracy of rotations (°) | 0.68 | 1.489 | |
| Accuracy of translations (pixels) | 0.655 | 0.881 | |
| Box size (pixels) | 512 | 512 | |
| Final resolution (Å) | 3.8 | 3.9 | |
| Map sharpening B factor (Å2) | −90 | −96 | |
| EMDB ID | 22093 | 22092 | 22090 |
| Refinement | |||
| Software | Phenix | ||
| Initial model (PDB code) | 6Q9D | 6Q9B and 1QRG | 6Q9D, 6Q9B and 1QRG |
| Map/model correlation | |||
| Model resolution (Å) | 3.9 | 4.0 | 3.9 |
| d99 (Å) | 3.9 | 4.0 | 4.0 |
| FSC model 0.5 (Å) | 3.9 | 3.9 | 3.9 |
| Map CC (around atoms) | 0.82 | 0.86 | 0.87 |
| Model composition | |||
| Non-hydrogen atoms | 26,001 | 19,052 | 45047 |
| Protein residues | 3284 | 2453 | 5736 |
| Number of chains | 17 | 18 | 34 |
| Number of ligands and cofactors | 11 | 1 | 12 |
| Number of lipids | 0 | 6 | 6 |
| Atomic Displacement Parameters (ADP) | |||
| Protein average (Å2) | 68.78 | 58.40 | 64.39 |
| Ligand average (Å2) | 48.59 | 48.59 | 48.59 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.007 | 0.007 | 0.007 |
| Bond angles (°) | 1.187 | 1.122 | 0.845 |
| Ramachandran Plot | |||
| Favored (%) | 82.90 | 88.03 | 84.98 |
| Allowed (%) | 16.76 | 11.88 | 14.79 |
| Disallowed (%) | 0.34 | 0.08 | 0.23 |
| Validation | |||
| MolProbity score | 2.41 | 2.31 | 2.38 |
| Clash score | 16.79 | 16.21 | 16.42 |
| Rotamer outliers (%) | 0.25 | 0.20 | 0.23 |
| EMRinger score | 1.47 | 2.09 | 2.17 |
| PDB ID | --- | --- | 6X89 |