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. Author manuscript; available in PMC: 2020 Apr 30.
Published in final edited form as: Nature. 2019 Oct 30;575(7781):234–237. doi: 10.1038/s41586-019-1703-4

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

FA core complex
(EMD-10290: consensus,
EMD-10291: top,
EMD-10292: middle,
EMD-10293: base)
(PDB 6SRI)
Subcomplex
(EMD-10294)
(PDB 6SRS)
Data collection and processing
Magnification 75,000 X 75,000 X
Voltage (keV) 300 300
Electron exposure (e−/Å2) 40 40
Defocus range (μm) -1.8 to -4.0 -1.8 to -4.0
Pixel size (Å) 1.040 (LMB) 1.040 (LMB)
1.085 (eBIC) 1.085 (eBIC)
Symmetry imposed CI CI
Initial particle images (no.) 1,947,765 1,947,765
Final particle images (no.) 169,000 49,423
Map resolution (Å) 4.2 (consensus), 4.5 (top),
4.4 (middle), 4.9 (base)
4.6
    FSC threshold 0.143 0.143
Map resolution range (Å) 4.2 to > 10 4.6 to > 10
Refinement
Initial model used De novo modelling and homology modelling De novo modelling and homology modelling
Model resolution range (Å) 4.5 (top), 4.4 (middle),
4.9 (base)
4.6
    FSC threshold 0.143 0.143
Model resolution range (Å) n/a n/a
Map sharpening B factor (Å2) -149 (consensus) -213
-198 (top)
-190 (middle)
-177 (bottom)
Model composition
    Non-hydrogen atoms 15,309 12,424
    Protein residues 3,827 3,106
    Ligands 0 0
B factors (Å2)
    Protein not estimated not estimated
    Ligands
R.m.s. deviations
    Bond lengths (Å) 0.23 0.22
    Bond angles (°) 0.48 0.50
Validation
   MolProbity score 1.44 1.12
   Clashscore 3 3
   Poor rotamers (%) 0 0
Ramachandran plot
   Favored (%) 95.95 98.88
   Allowed (%) 3.56 1.12
   Disallowed (%) 0.49 0