Table 1. Cryo-EM data collection, refinement, and validation statistics.
| PDB ID EMDB ID |
CMZ-bound hTRPC5 7D4P EMD-30575 |
HC-070-bound hTRPC5 7D4Q EMD-30576 |
apo_hTRPC5 |
|---|---|---|---|
| 7E4T | |||
| EMD-30987 | |||
| Data collection and processing | |||
| Magnification | 130,000× | 165,000× | 130,000× |
| Voltage (kV) | 300 | 300 | 300 |
| Electron exposure (e-/Å2) | 50 | 50 | 50 |
| Defocus range (μm) | −1.5 to −2.0 | −1.5 to −2.0 | −1.5 to −2.0 |
| Pixel size (Å) | 1.045 | 0.821 | 1.045 |
| Symmetry imposed | C4 | C4 | C4 |
| Initial particle images (no.) | 354,312 | 274,189 | 64,918 |
| Final particle images (no.) | 90,357 | 114,211 | 29,156 |
| Map resolution (Å) Fourier shell correlation threshold |
2.7 0.143 |
2.7 0.143 |
3.0 0.143 |
| Map resolution range (Å) | 250–2.7 | 250–2.7 | 250–3.0 |
| Refinement | |||
| Initial model used (PDB code) | 5Z96 | 5Z96 | 5Z96 |
| Model resolution (Å) Fourier shell correlation threshold |
2.7 0.143 |
2.7 0.143 |
3.0 0.143 |
| Model resolution range (Å) | 250–2.7 | 250–2.7 | 250–3.0 |
| Map sharpening B factor (Å2) | −119.0 | −118.1 | −119.0 |
| Model composition | |||
| Nonhydrogen atoms Protein residues Ligands |
22,472 2680 28 |
22,388 2672 24 |
22,276 2656 24 |
| B factors (Å2) | |||
| Protein ligand |
95.86 91.34 |
120.29 124.44 |
140.20 133.98 |
| Root-mean-square deviations | |||
|
Bond lengths (Å) Bond angles (°) |
0.004 0.914 |
0.004 0.918 |
0.004 0.906 |
| Validation | |||
| Validation MolProbity score Clashscore Poor rotamers (%) |
1.21 4.33 0.67 |
1.32 5.80 0.67 |
1.30 5.52 1.01 |
| Ramachandran plot | |||
| Favored (%) Allowed (%) Disallowed (%) |
98.78 1.22 0.00 |
98.63 1.37 0.00 |
98.93 1.07 0.00 |