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. Author manuscript; available in PMC: 2020 Aug 17.
Published in final edited form as: Nat Struct Mol Biol. 2020 Feb 17;27(3):233–239. doi: 10.1038/s41594-020-0379-7

Table 2. Cryo-EM data collection, refinement and validation statistics.

Smc3–Scc1–CtSmc1
complex
(EMD-4614, PDB 6QPW)
Data collection and processing
Magnification 165,000
Voltage (kV) 300
Electron exposure (e2) 42.08
Defocus range (μm) 1.25-2.5
Pixel size (Å) 0.81
Symmetry imposed C1
Initial particle images (no.) 290,821
Final particle images (no.) 178,162
Map resolution (Å) 3.2
    FSC threshold 0.143
Map resolution range (Å) 3.2-10
Refinement
Initial model used (PDB code) 4UX3, 6QPQ
Model resolution (Å) 3.2
    FSC threshold 0.143
Model resolution range (Å) 3.2-10
Map sharpening B factor (Å2) -124
Model composition
   Nonhydrogen atoms 6784
   Protein residues 839
   Ligands 4
B factors (Å2)
   Protein 85.99
   Ligand 53.76
R.m.s. deviations
    Bond lengths (Å) 0.005
    Bond angles (°) 0.987
Validation
MolProbity score 1.66
Clashscore 5.83
Poor rotamers (%) 0.14
Ramachandran plot
    Favored (%) 95.02
    Allowed (%) 4.92
    Disallowed (%) 0.00