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. Author manuscript; available in PMC: 2020 Mar 30.
Published in final edited form as: Nat Struct Mol Biol. 2019 Sep 30;26(10):919–929. doi: 10.1038/s41594-019-0297-8

Table 1.

Cryo-EM data collection, refinement and validation statistics

RNCRodZ•SecA (EMDB-10073, PDB 6S0K) SecA (local refinement) (EMDB-10074)
Data collection and processing
Magnification 100,719 100,719
Voltage (kV) 300 300
Electron exposure (e–/Å2) 40 40
Defocus range (μm) 1.5 – 2.8 1.5 – 2.8
Pixel size (Å) 1.39 1.39
Symmetry imposed C1 C1
Initial particle images (no.) 2,613,025 2,613,025
Final particle images (no.) 37,334 37,334
Map resolution (Å) 3.1 5.7
 FSC threshold 0.143 0.143
Map resolution range (Å) 2.9 – 9.5 5.5 – 9.5
Refinement
Initial model used (PDB code) 5GAG, 2FSF, 2VDA
Model resolution (Å) 3.3
 FSC threshold 0.5
Model resolution range (Å)
Map sharpening B factor (Å2) –130.53
Model composition
 Non-hydrogen atoms 98,708
 Protein residues 4,384
 Nucleic acid residues 3,006
 Ligands 69
B factors (Å2)
 Protein 148.63
 Nucleotide 95.06
 Ligand 60.40
R.m.s. deviations
 Bond lengths (Å) 0.005
 Bond angles (°) 0.776
Validation
MolProbity score 1.52
Clashscore 4.21
Poor rotamers (%) 0.73
Ramachandran plot
 Favored (%) 95.44
 Allowed (%) 4.28
 Disallowed (%) 0.28