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. Author manuscript; available in PMC: 2020 Jan 8.
Published in final edited form as: Nat Struct Mol Biol. 2019 Oct 28;26(11):1013–1022. doi: 10.1038/s41594-019-0319-6

Table 1 |. Cryo-EM data collection, refinement and validation statistics.

STC-C2 (EMD-20254, PDB 6P5A) STC-C1 (EMD-20321, PDB 6PE2)
Data collection and processing
 Magnification 35,000 35,000
 Voltage (kV) 200 200
 Electron exposure (e Å−2) 60 60
 Defocus range (μm) −1 to −3 μm −1 to −3 μm
 Pixel size (Å) 1.16 1.16
 Symmetry imposed C2 C1
 Initial particle images (no.) 547,929 547,929
 Final particle images (no.) 252,574 252,574
 Map resolution (Å)/FSC threshold 3.6/0.143 3.9/0.143
 Map resolution range (Å) 3–5 4–10
Refinement
 Initial model used - 6P5A
 Model resolution (Å)/FSC threshold 3.7/0.5 4/0.5
 Model resolution range (Å) - -
 Map sharpening B factor (Å2) 100 100
 Model composition
 Non-hydrogen atoms 11,956 12,753
 Protein residues 1,120 1,148
 Ligands 6 6
B factors (Å2)
 Protein 47.13 185.97
 Ligand 38.87 171.81
R.m.s. deviations
 Bond lengths (Å) 0.008 0.003
 Bond angles (°) 0.52 0.532
Validation
 MolProbity score 1.22 1.56
 Clashscore 4.46 6.4
 Poor rotamers (%) 0% 0%
Ramachandran plot
 Favored (%) 98% 96.75%
 Allowed (%) 2% 3.25%
 Disallowed (%) 0% 0%