Table 1 Cryo-EM data collection, refinement and validation statistics
From: Structural basis of the human NAIP/NLRC4 inflammasome assembly and pathogen sensing
Data collection and processing | |||
Magnification | ×150,000 | ×150,000 | ×150,000 |
Voltage (kV) | 200 | 200 | 200 |
Electron exposure (e− Å−2) | 43.8 | 43.8 | 43.8 |
Defocus range (μm) | −0.8 to −2.4 | −0.8 to −2.4 | −0.8 to −2.4 |
Pixel size (Å) | 0.948 | 0.948 | 0.948 |
Symmetry imposed | C11 (Global) C1 (Focus) | C11 (Global) C1 (Focus) | C1 |
Initial particle images (no.) | 128,266 | 128,266 | 869,012 |
Final particle images (no.) | 72,822 | 21,406 | 106,381 |
Map resolution (Å) | 3.80 | 4.46 | 3.60 |
FSC threshold | 0.143 | 0.143 | 0.143 |
Map resolution range (Å) | 3.5–8.0 | 4.4–9.0 | 3.3–6.0 |
Refinement | |||
Initial model used (PDB code) | SWISS-MODEL | SWISS-MODEL | SWISS-MODEL |
Model resolution (Å) | 4.0 | 5.0 | 3.7 |
FSC threshold | 0.5 | 0.5 | 0.5 |
Model resolution range (Å) | 4.0–6.0 | 5.0–7.0 | 3.7–6.0 |
Map sharpening B factor (Å2) | −106.4 | −148.4 | −95.4 |
Model composition | |||
Non-hydrogen atoms | 2,700 | 2,700 | 2,334 |
Protein residues | ATP,1 | ||
Ligands | |||
B factors (Å2) | |||
Protein | 80.9 | 213.1 | 68.3 |
Ligand | 26.9 | ||
r.m.s.d. | |||
Bond lengths (Å) | 0.0109 | 0.0114 | 0.0113 |
Bond angles (°) | 0.96 | 0.98 | 1.01 |
Validation | |||
MolProbity score | 1.26 | 1.30 | 1.49 |
Clashscore | 1.31 | 1.56 | 2.21 |
Poor rotamers (%) | 0.17% | 0.08% | 0.00% |
Ramachandran plot | |||
Favored (%) | 93.96% | 94.07% | 91.73% |
Allowed (%) | 5.30% | 5.07% | 6.86% |
Disallowed (%) | 0.74% | 0.85% | 1.41% |
