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. Author manuscript; available in PMC: 2022 Jul 1.
Published in final edited form as: Nat Struct Mol Biol. 2021 Dec 30;29(1):40–46. doi: 10.1038/s41594-021-00699-y

Table 1.

Cryo-EM data collection, refinement and validation statistics.

CNGA3/CNGB3 apo (EMD-24468, PDB 7RHS)

Data collection and processing
Magnification 105,000 ×
Voltage (kV) 300
Electron exposure (e/Å2) 57.63
Defocus range (μm) −0.6 to −2.2
Pixel size (Å) 0.8247
Symmetry imposed C1
Initial particle images (no.) 3,982,214
Final particle images (no.) 205,492
Map resolution (Å) 2.93
 FSC threshold 0.143
Map resolution range (Å) 2.7 to 3.1
Refinement
Initial model used De novo structure
Model resolution (Å) 3.06
 FSC threshold 0.143
Map sharpening B factor (Å2) −103
Model composition
 Non-hydrogen atoms 14,767
 Protein residues 1,804
 Sugar moieties 3
 Ion (Na+) 1
B factors (Å2)
 Protein 85.39
 Sugar moieties 89.59
R.m.s. deviations
 Bond lengths (Å) 0.006
 Bond angles (°) 0.945
Validation
 MolProbity score 1.28
 Clashscore 3.47
 Poor rotamers (%) 0.06
Ramachandran plot
 Favored (%) 97.22
 Allowed (%) 2.78
 Disallowed (%) 0