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. Author manuscript; available in PMC: 2020 Feb 26.
Published in final edited form as: Nat Struct Mol Biol. 2019 Aug 26;26(9):823–829. doi: 10.1038/s41594-019-0286-y

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

Motor domain
(EMD-4917, PDB 6RLA)
Tail
(EMD-4918, PDB 6RLB)
Data collection and processing
Magnification 105,000 105,000
Voltage (kV) 300 300
Electron exposure (e2) 49.6a, 46.8b, 45.4c 49.6a, 46.8b, 45.4c
Defocus range (μm) –1 to –3.5 –1 to –3.5
Pixel size (Å) 1.39 1.39
Symmetry imposed C2 C1
Initial particle images (no.) 229,969 461,684
Final particle images (no.) 57,265 68,623
Map resolution (Å) 3.9 4.5
    FSC threshold 0.143 0.143
Map resolution range (Å) 3.7–5.5 4.3–8.0
Refinement
Initial model used (PDB code) 4RH7 5OWO, 6F1T,
6F1Y, 6F1U,
6F1Z, 2PG1,
2XQQ & de novo
Model resolution (Å) 3.8 4.5
    FSC threshold 0.143 0.143
Model resolution range (Å) 3.7–5.5 4.3–8.0
Map sharpening B factor (Å2) –100 –125
Model composition
    Nonhydrogen atoms 43,034 20,408
    Protein residues 5,500 4,122
    Ligands ADP: 6, ATP: 2, Mg: 2 0
R.m.s. deviations
    Bond lengths (Å) 0.007 0.007
    Bond angles (°) 1.141 0.951
Validation
MolProbity score 1.65 backbone model
Clashscore 3.81 0.41
Poor rotamers (%) 0.35 backbone model
Ramachandran plot
    Favored (%) 92.07 95.91
    Allowed (%) 7.93 4.04
    Disallowed (%) 0 0.05

Dataset 1a, 2b, 3c