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. Author manuscript; available in PMC: 2020 May 8.
Published in final edited form as: J Mol Biol. 2019 Aug 17;431(22):4444–4454. doi: 10.1016/j.jmb.2019.08.003

Table 1.

Cryo-EM data collection, reconstruction, and modeling statistics

Data collection Data Collection 1 Data Collection 2
Microscope Titan Krios Titan Krios
Voltage (kV) 300 300
Magnification 130,000X 130,000X
Camera K2 Summit K2 Summit
Energy filter slit 20 eV 20 eV
Defocus range 1.2–2.2 (underfocus) 1.5–2.5 (underfocus)
Pixel size 1.0605 1.0605
Images (number) 3260 3711
Reconstruction CBF3 core CBF3 Ndc10 D1 CBF3 Ndc10 D1D2
Particles 130,143 63,177 63,177
Box size 288 288 288
Accuracy of rotations 2.56 3.32 2.27
Accuracy of translations 0.91 1.23 1.41
Map resolution—FSC threshold 0.143 3.97 4.07 4.30
Map sharpening B factor 100 80 10
Model refinement and statistics
Refinement resolution 4.0 4.1
CC (mask) 0.7985 0.78
R.M.S. deviations
 Bond lengths 0.011 0.007
 Bond angles 1.199 0.942
Validation
 MolProbity scores 1.91 1.96
 Clashscore 6.57 6.86
 Favored rotamers 95.34% 95.81%
 Poor rotamers 0.08% 0.07%
 Cbeta deviations 0.25Å 0 0
Ramachandran plot
 Favored (%) 89.99% 88.63%
 Allowed (%) 9.79% 11.10%
 Disallowed (%) 0.22% 0.27%
Peptide omega
 Cis prolines (%) 0.00% 0.00%
 Twisted peptides 0.15% 0.20%

FSC, Fourier shell correlation