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. Author manuscript; available in PMC: 2021 Sep 30.
Published in final edited form as: Nat Struct Mol Biol. 2020 Feb 10;27(2):202–209. doi: 10.1038/s41594-020-0373-0

Table 2 |.

Cryo-EM data collection, model refinement and validation statistics

Apo mBcs1 (EMD-20808, PDB 6UKP) ATPγS-bound mBcs1 (EMD-20811, PDB 6UKS)

Data collection and processing
Magnification ×14,000 ×14,000
Voltage (kV) 300 300
Electron exposure (e-2) 40 40
Defocus range (μm) −1.25 to −2.5 −1.25 to −2.5
Pixel size (Å) 0.86 0.86
Symmetry imposed C7 C7
Initial particle images (no.) 560,780 3,888,212
Final particle images (no.) 67,261 95,674
Map resolution (Å) 3.81 3.2
 FSC threshold 0.143 0.143
Map resolution range (Å) 3.5–12 3.0–12
Refinement
Initial model used (PDB code) Bcs1-specific domain built de novo AAA domain built de novo
Model resolution (Å) 4.1 3.8
FSC threshold 0.5 0.5
Map sharpening B factor (Å2) −46.1 −20.18
Model composition
 Nonhydrogen atoms 41,132 40,929
 Protein residues 2,569 2,534
 Ligands - 14 (7 ATPγS, 7 Mg2+)
B factors (Å2)
 Protein 107.76 82.94
 Ligand - 59.10
r.m.s. deviations
 Bond lengths (Å) 0.006 0.007
 Bond angles (°) 1.035 0.857
Validation
MolProbity score 1.62 1.45
Clashscore 2.72 1.88
Poor rotamers (%) 0 0
Ramachandran plot
 Favored (%) 89.53 91.62
 Allowed (%) 10.47 8.38
 Disallowed (%) 0 0