Table 1.
Cryo-EM data collection and refinement statistics
| Sen1FL | Sen1Sen1N | Sen1N-PP-C | |
|---|---|---|---|
| EMDB | EMD-29439 | EMD-29440 | EMD-29426 |
| PDB ID | 8FTK | n/a | 8FTH |
| Data collection and processing | |||
| Microscope | Titan Krios | Titan Krios | Titan Krios |
| Detector | K2 summit | K2 summit | Gatan3 Bioquantum |
| Magnification | 130,000 | 130,000 | 130,000 |
| Voltage(kV) | 300 | 300 | 300 |
| Electron exposure (e–/Å2) | 60 | 60 | 40 |
| Defocus range (μm) | −1.4 to −2.2 | −1.4 to −2.2 | −1.0 to −2.7 |
| Pixel size (Å) | 0.53 | 0.53 | 0.67 |
| Symmetry imposed | C1 | C1 | C1 |
| Number of micrographs | 5089 | 5089 | 6379 (set1) + 3655 (set2) |
| Initial particle images (no.) | 1351862 | 1351862 | 3400325 (set1) + 3273289 (set2) |
| Final particle images (no.) | 29391 | 74760 | 471395 |
| Map resolution - unmaksed (Å) (FSC = 0.143) | 7.40 | 6.86 | 3.69 |
| Map resolution -masked (Å) (FSC = 0.143) | 4.56 | 4.49 | 3.17 |
| Refinement | |||
| Initial models used (PDB code) | AlphaFold (1-900), CtSen1Hel X-ray | No model refined | AlphaFold (1-900), CtSen1Hel X-ray |
| Map sharpening B factor (Å2) | 122.6 | 142.5 | |
| Model composition | Polyalanine | ||
| Nonhydrogen atoms | 7840 | 9778 | |
| Protein residues | 1584 | 1263 | |
| ADP nucleotides | 0 | 1 | |
| B factors (Å2) (mean) | |||
| Protein | 219.90 | 56.70 | |
| Nucleotide | n/a | 40.90 | |
| R.M.S. deviations | |||
| Bond lengths (Å) | 0.002 | 0.008 | |
| Bond angles (°) | 0.573 | 1.266 | |
| Map-model CC | |||
| CC (mask) | 0.81 | 0.75 | |
| CC (volume) | 0.80 | 0.72 | |
| CC (peaks) | 0.74 | 0.61 | |
| Validation | |||
| Molprobity score | 1.60 | 1.60 | |
| Clashscore | 4.21 | 4.89 | |
| Poor rotamers (%) | 0.00 | 0.49 | |
| Ramachandran plot | |||
| Outliers (%) | 0.00 | 0.00 | |
| Allowed (%) | 5.86 | 4.87 | |
| Favored (%) | 94.14 | 95.13 | |