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. Author manuscript; available in PMC: 2020 May 13.
Published in final edited form as: Nature. 2019 Nov 13;575(7783):540–544. doi: 10.1038/s41586-019-1753-7

Extended Data Table 2.

Statistics of cryo-EM data collection, refinement and validation

PRC (intact TIR) (EMD-20452) (PDB 6PQR) PRC (nicked TIR) (EMD-20453) (PDB 6PQU) HFC (EMD-20455) (PDB 6PQX) TEC (EMD-20456) (PDB 6PQY) STC (EMD-20457) (PDB 6PR5)
Data collection and processing
Magnification 130,000 130,000 130,000 130,000 130,000
Voltage (kV) 300 300 300 300 300
Electron exposure (e2) 50.8 52.2 52.2 54.4 54.4
Defocus range (μm) −1.5–−2.5 −1.5–−2.5 −1.5–−2.5 −1.5–−2.5 −1.5–−2.5
Pixel size (Å) 1.05 1.05 1.05 1.05 1.05
Symmetry imposed C2 C2 C2 C2 C1
Initial particle images (no.) 243,518 300,406 262,691 228,413 228,413
Final particle images (no.) 32,984 59,333 3,997 26,397 43,661
Map resolution (Å) 3.4 3.3 4.6 4.2 3.3
 FSC threshold 0.143 0.143 0.143 0.143 0.143
Map resolution range (Å) 2.4–5.2 2.4–5.6 4.0–8.0 3.7–6.8 2.5–5.6
Refinement
Initial model used (PDB code) 6PQN 6PQN 6PQN 6PQN 6PQN
Model resolution (Å) 3.7 3.6 4.8 4.7 3.5
 FSC threshold 0.5 0.5 0.5 0.5 0.5
Model resolution range (Å) 2.4–5.2 2.4–5.6 4.0–8.0 3.7–6.8 2.5–5.6
Map sharpening B factor (Å2) −90 −90 −126 −120 −90
Model composition
 Non-hydrogen atoms 9266 10004 10116 8690 10194
 Protein residues 936 936 960 920 960
 Nucleotides 88 124 120 64 124
 Ligands 6 6 4 0 6
B factors (Å2)
 Protein 105.51 74.58 89.52 182.34 59.68
 Nucleic acid 104.92 131.57 160.90 158.19 91.35
 Ligand 109.58 93.13 81.45 69.54
R.m.s. deviations
 Bond lengths (Å) 0.009 0.008 0.006 0.007 0.008
 Bond angles (°) 0.830 0.890 0.984 0.980 0.768
Validation
 MolProbity score 1.91 2.04 2.39 2.35 1.64
 Clashscore 16.01 23.12 16.06 24.55 13.64
 Poor rotamers (%) 0.24 1.21 2.35 0.49 0.71
Ramachandran plot
 Favored (%) 96.74 97.39 94.14 92.51 98.33
 Allowed (%) 3.26 2.39 5.23 6.83 1.36
 Disallowed (%) 0 0.22 0.63 0.66 0.31