Table 1 Cryo-EM data collection, refinement and validation statistics.
2 mg ml−1 hTRPC5 | 1 mg ml−1 hTRPC5 | 1 mg ml−1 hTRPC5 | |
|---|---|---|---|
100 µM Pico145 (EMDB-10903) (PDB 6ysn) | 50 µM Pico145 (EMDB-10909) | 20 µM ZnCl2 (EMDB-10910) | |
Data collection and processing | |||
Magnification | 130,000 | 130,000 | 130,000 |
Voltage (kV) | 300 | 300 | 300 |
Electron exposure (e–/Å2) | 75 | 60 | 60 |
Defocus range (μm) | −1 to −3 | −1 to −3 | −1 to −3 |
Pixel size (Å) | 1.07 | 1.07 | 1.07 |
Symmetry imposed | C4 | C4 | C4 |
Initial particle images (no.) | 612,983 | 536,348 | 552,075 |
Final particle images (no.) | 158,111 | 158,548 | 228,615 |
Map resolution (Å) | 3.0 | 2.9 | 2.8 |
FSC threshold | 0.143 | 0.143 | 0.143 |
Map resolution range (Å) | 2.8–3.6 | 2.7–3.5 | 2.6–3.5 |
Refinement | |||
Initial model used (PDB code) | 6aei | ||
Model resolution (Å) | 3.0 | ||
FSC threshold | 0.143 | ||
Model resolution range (Å) | 2.8–3.6 | ||
Map sharpening B factor (Å2) | −100 | ||
Model composition | |||
Non-hydrogen atoms | 19,700 | ||
Protein residues | 2504 | ||
Ligands | 4 | ||
B factors (Å2) | |||
Protein | 61.67 | ||
Ligand | 22.44 | ||
R.m.s. deviations | |||
Bond lengths (Å) | 0.005 | ||
Bond angles (°) | 0.657 | ||
Validation | |||
MolProbity score | 1.68 | ||
Clashscore | 5.28 | ||
Poor rotamers (%) | 0.19 | ||
Ramachandran plot | |||
Favoured (%) | 94.07 | ||
Allowed (%) | 5.93 | ||
Disallowed (%) | 0.0 | ||
