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. Author manuscript; available in PMC: 2024 May 6.
Published in final edited form as: Nat Struct Mol Biol. 2022 Feb 24;29(3):210–217. doi: 10.1038/s41594-022-00727-5

Extended Data Table 1 |.

Cryo-EM data collection, refinement and validation statistics

SSTR2/Octreotide/Gi3/scFv16 SSTR2/SST14/Gi3/scFv16
Data collection and processing
Magnification (x) 57,050 57,050
Voltage (kV) 300 300
Electron exposure (e−/Å2) 67.00 52.00
Defocus range (μm) −0.8 to −1.8 −0.8 to −1.8
Pixel size (Å) 0.8521 0.8521
Symmetry imposed C1 C1
Initial particle images (no.) 6,860,866 4,464,832
Final particle images (no.) 281,479 442,863
Map resolution (Å) 2.9 2.5
 FSC threshold 0.143 0.143
Refinement
Model Resolution 2.9 2.5
FSC Threshold 0.143 0.143
Model Composition
 Non-hydrogen Atoms
8215 8428
 Protein Atoms 8215 8423
 Waters & Ions
B factor (Å2)
0 5
 Protein Atoms 46.84 52.86
 Waters & Ions 49.20
R.M.S Deviations
 Bonds (Å)
0.005 0.005
 Angles (º) 0.907 0.997
Validation
 MolProbity score
1.58 1.33
 Clashscore 5.26 3.49
 Poor rotamers (%) 0.13 0.73
Ramachandran Plot
 Favored (%)
95.69 96.89
 Allowed (%) 4.31 3.02
 Outliers (%) 0.00 0.09