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. Author manuscript; available in PMC: 2024 Jul 3.
Published in final edited form as: Nat Struct Mol Biol. 2024 Feb 7;31(4):667–677. doi: 10.1038/s41594-024-01223-8

Table 1:

Cryo-EM data collection and model statistics.

GPR161-Gs (EMDB-40603) (PDB 8SMV)
Data collection and processing
Magnification 105,000
Voltage (kV) 300
Electron exposure (e–/Å2) 50.7
Defocus range (μm) −0.8 to −2.2
Pixel size (Å) 0.86
Symmetry imposed C1
Initial particle images (no.) 9,760,777
Final particle images (no.) 335,928
Map resolution (Å)
 FSC threshold		 2.7
0.143
Map resolution range (Å) 2.7–5.4
Refinement
Initial model used Alphafold2 model
Model resolution (Å)
 FSC threshold		 3.1
0.5
Model resolution range (Å) 3.1–50
Map sharpening B factor (Å2) −119
Model composition
 Non-hydrogen atoms
 Protein residues
 Ligands		  
8,169
1,034
1
B factors (Å2)
 Protein (GPR161)
 Protein (G protein/Nb35)
 Ligand (cholesterol)		  
45.0
21.6
53.5
R.m.s. deviations
 Bond lengths (Å)
 Bond angles (°)		  
0.004
1.033
Validation
 MolProbity score
 Clashscore
 Poor rotamers (%)		  
1.12
1.86
0
Ramachandran plot
 Favored (%)
 Allowed (%)
 Disallowed (%)		  
96.96
3.04
0