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. Author manuscript; available in PMC: 2018 Jun 4.
Published in final edited form as: Nat Struct Mol Biol. 2017 Dec 4;25(1):37–44. doi: 10.1038/s41594-017-0003-7

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

hINO80 core complex (EMD-3772) High resolution hINO80 sub-complex (EMD-3773 PDB 5OAF) SC2 (EMD-3774) SC2plus (EMD-3775)
Data collection and processing
Magnification 123,000 123,000 62,000 62,000
Voltage (kV) 300 300 200 200
Electron exposure (e–/Å2) 45-50 45 43 50
Defocus range (μm) -1.0 to -3.5 -1.2 to -3.2 -1.3 to -4.5 -1.0 to -4.0
Pixel size (Å) 2.26 1.06 3.30 3.30
Symmetry imposed none none none none
Initial particle images (no.) 367,000 304,304 231,000 96,533
Final particle images (no.) 11,496 104,214 74,226 85,989
Map resolution (Å) 9.6 4.1 11.5 8.4
    FSC threshold 0.143 0.143 0.143 0.143
Map resolution range (Å) ~7 to ~15 ~3 to ~8 ~10 to ~15 ~8 to ~11
Refinement
Initial model used 4WVY
Model resolution (Å) 4.1
    FSC threshold 0.143
Model resolution range (Å) 4-8
Map sharpening B factor (Å2) -140
Model composition
    Nonhydrogen atoms 19748
    Protein residues 2,538
    Ligands 6
B factors (Å2)
    Protein 75
    Ligand 28
R.m.s. deviations
    Bond lengths (Å) 0.23
    Bond angles (°) 0.41
 Validation
    MolProbity score
    Clashscore 12.2
    Poor rotamers (%) 0.00
Ramachandran plot
    Favored (%) 97.6
    Allowed (%) 2.4
    Disallowed (%) 0