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. 2022 Jun 14;41(18):e109990. doi: 10.15252/embj.2021109990

Table 1.

Cryo‐EM data collection, refinement, and validation statistics.

Specifications TqsA (EMDB: 12256) (PDB:7NB6) YdiK (EMDB: 13057) (PDB:7OT9)
Data collection and processing
Magnification 105,000 105,000
Voltage (kV) 300 300
Electron exposure (e2) 80 80
Defocus range (μm) −1.1 to −2.1 −1.1 to −2.1
Pixel size (Å) 0.837 0.831
Symmetry imposed C5 C5
Initial particle images (no.) 1,218,552 1,222,739
Final particle images (no.) 134,300 619,311
Map resolution (Å) 3.35 2.80
FSC threshold 0.143 0.143
Map resolution range (Å) 3.0–7.2 2.6–6.5
Refinement
Initial model used
Model resolution (Å) 2.9 2.5
FSC threshold 0.143 0.143
Map sharpening B factor (Å2) −30 −10
Model composition
Non‐hydrogen atoms 13,020 8,410
Protein/nucleotide residues 1,700 1,105
Ligands
B factors (Å2) (min/max/mean)
Protein 18.22/197.18/109.91 71.51/175.24/100.68
Ligands
R.m.s deviations
Bond lengths (Å) 0.010 0.006
Bond angles (°) 1.282 1.002
Validation
MolProbity score 2.13 1.90
Clashscore 13.42 9.94
Poor rotamers (%) 0.49 0
CaBLAM outliers (%) 2.38 2.39
Ramachandran Plot
Favored (%) 91.72 94.42
Allowed (%) 8.28 5.58
Disallowed (%) 0 0