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

From: Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD

  RNAP elongation complex (EMD-21920, PDB 6WVJ) RNAP-HelD complex (EMD-21921, PDB 6WVK)
Data collection and processing
Molecular mass (kDa) 344.200 442.060
Magnification 59,524 59,524
Voltage (kV) 300 300
Electron exposure (eÅ−2) 52.2 63.6
Defocus range (μm) 0.6–2.8 0.6–2.8
Pixel size (Å) 0.84 0.84
Symmetry imposed C1 C1
Initial particle images (no.) 1069336 580,468
Final particle images (no.) 58,854 65,356
Relative abundance (%) 5.5% 11.2%
Map resolution (Å) 3.36 3.36
FSC threshold 0.143 0.143
Dimensions (Length × width × hight in Å) 150 × 112 × 123 156 × 154 × 139
Refinement
Initial model used 6WVK 4NJC (ε)
Model resolution (Å) 3.38 3.27
FSC threshold 0.5 0.5
Model composition
Non-hydrogen atoms 22367 28225
Protein residues 2802 3631
Nucleic acid residues 37
Ligands ZN: 2, MG: 1 ZN: 2, MG: 1
B Factors (Å2)
Protein 63.03 46.39
Nucleic 111.00
Ligand 86.05 68.02
r.m.s deviations
Bond lengths (Å) 0.005 0.005
Bond angles (°) 0.692 0.774
Validation
MolProbity score 2.61 2.69
Clashscore 12.44 10.95
Poor rotamers (%) 5.49 6.70
Ramachandran plot
Favoured (%) 93.14 91.42
Allowed (%) 6.75 8.39
Disallowed (%) 0.11 0.19