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. Author manuscript; available in PMC: 2019 May 26.
Published in final edited form as: Nat Struct Mol Biol. 2018 Nov 26;25(12):1103–1110. doi: 10.1038/s41594-018-0154-1

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

CBF3core−Ndc10DBD
(EMD-0095, PDB 6GYP)
CBF3−CEN3
(EMD-0096, PDB 6GYS)
CBF3msk
(EMD-0099, PDB 6GYU)
Data collection and processing
Magnification 132,075 132,075 132,075
Voltage (kV) 300 300 300
Electron exposure (e2) ~28 ~28 ~28
Defocus range (μm) 2.4-3.5 2.4-3.5 2.4-3.5
Pixel size (Å) 1.06 1.06 1.06
Symmetry imposed C1 C1 C1
Initial particle images (no.) 757,433 987,484 987,484
Final particle images (no.) 73,894 22,668 198,010
Map resolution (Å) 3.6 4.4 3.0
    FSC threshold 0.143 0.143 0.143
Map resolution range (Å) 3.3-4.5 3.7-8.3 2.5-3.7
Refinement
Initial model used (PDB code) 2QUQ,4ACO,1FQV,2HAP 2QUQ,4ACO,1FQV,2HAP 2QUQ,1FQV,2HAP
Model resolution (Å) 3.6 4.4 3.0
    FSC threshold 0.143 0.143 0.143
Model resolution range (Å)
Map sharpening B factor (Å2) -120 -110 -120
Model composition
    Non-hydrogen atoms 17,811 38,882 18,157
    Protein residues 2,800 5,688 2,800
    Ligands 0 8 2
B factors (Å2)
    Protein 174.4 304.1 148.9
    Ligand - 395.4 181.3
R.m.s. deviations 0.006 0.007 0.005
    Bond lengths (Å) 0.895 1.018 0.872
    Bond angles (°) 0.693 0.811 0.780
Validation
MolProbity score 1.71 1.77 1.72
Clashscore 4.86 6.07 5.00
Poor rotamers (%) 0.50 0.29 0.74
Ramachandran plot
    Favored (%) 92.83 93.36 93.58
    Allowed (%) 7.08 6.48 6.28
    Disallowed (%) 0.09 0.16 0.14