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. Author manuscript; available in PMC: 2022 Oct 1.
Published in final edited form as: Nat Struct Mol Biol. 2022 Mar 24;29(4):348–356. doi: 10.1038/s41594-022-00748-0

Table 1.

Cryo-EM data collection, refinement, and validations

Active state
(EMBD-24784)
(PDB 7S05)
Autoinhibited state
(EMBD-24785)
(PDB 7S06)
Data collection and processing
Magnification 130,000
Voltage (kV) 300
Electron exposure (e2) 66
Defocus rang (μm) 1.0–2.3
Pixel size (Å) 0.828
Symmetry imposed C2
Initial particle images (No.) 5,186,047
Final particle images (No.) 365,927 66,173
Map resolution (Å) 3.1 3.3
 FSC threshold 0.143 0.143
Map resolution range (Å) 2.0 – 5.0 2.0 – 5.0
Refinement
Initial model used (PDB code) -- --
Model resolution (Å) 3.2 3.5
 FSC threshold 0.5 0.5
Model resolution range (Å) 2–5 2–5
Map sharpening B factor (Å2) −150.5 −141
Model composition
 Non-hydrogen atoms 7504 7850
 Protein residues 874 918
 Ligands 16 14
B factors (Å2)
 Protein 58.4 90.2
 Ligand 81.7 123.2
R.m.s. deviations
 Bond lengths (Å) 0.003 0.003
 Bond angles (°) 0.653 0.620
Validation
 Molprobity score 1.79 1.82
 Clashscore 7.23 7.56
 Poor rotamers (%) 0 0
Ramachandran plot
 Favored (%) 94.17 93.99
 Allowed (%) 5.83 6.01
 Disallowed (%) 0 0