Table 1 Cryo-EM data collection and model statistics
From: Engineering of a mammalian VMAT2 for cryo-EM analysis results in non-canonical protein folding
| Â | OaVMAT2TM8/9-BRIL (EMD-38389) (PDB: 8XIT) | XlVMAT2WT (EMD-38390) (PDB: 8XIU) |
|---|---|---|
Data collection and processing | ||
 Movies | 6149 | 8192 |
 Magnification | 165,000× | 165,000× |
 Voltage (kV) | 300 | 300 |
 Electron exposure (e–/Å2) | 62.64 | 59.1 |
 Defocus range (μm) | −1.0 to −1.6 | −1.1 to −1.6 |
 Pixel size (Å) | 0.85 | 0.85 |
 Symmetry imposed | C2 | - |
 Initial particle images (no.) | 1,064,611 | 1,272,193 |
 Final particle images (no.) | 304,899 | 107,961 |
 Map resolution (Å) | 3.2 | 4.0 |
  FSC threshold | 0.143 | 0.143 |
Refinement | ||
Model composition | Â | Â |
  Non-hydrogen atoms | 6002 | 2615 |
  Protein residues | 784 | 348 |
  Ligands | - | - |
R.m.s. deviations | ||
  Bond lengths (Å) | 0.003 | 0.002 |
  Bond angles (°) | 0.644 | 0.554 |
Validation | ||
  MolProbity score | 1.22 | 1.35 |
  Clashscore | 4.42 | 5.99 |
  Rotamer outliers (%) | 0.00 | 0.00 |
Ramachandran plot | ||
  Favored (%) | 98.02 | 98.51 |
  Allowed (%) | 1.98 | 1.49 |
  Disallowed (%) | 0.00 | 0.00 |
B-factors (Ã…2) | ||
  Protein | 80.42 | 139.87 |
  Ligand | - | - |
