Table 1 Cryo-EM data collection, refinement and validation statistics
From: Structural basis for the synergistic assembly of the snRNA export complex
Data collection and processing | |||
Magnification | 105,000× | ||
Voltage (kV) | 300 | ||
Electron exposure (e– Å−2) | 40.5 | ||
Defocus range (μm) | −1.0 to −2.2 | ||
Pixel size (Å) | 0.84 | ||
Symmetry imposed | – | ||
Initial particle images (no.) | 1,778,233 | ||
Final particle images (no.) | 204,250 | ||
Complete, map | Focused map, CBC | Focused map, CRM1 | |
Map resolution (Å) | 2.62 | 2.44 | 2.43 |
FSC threshold | 0.143 | 0.143 | 0.143 |
Map resolution range (Å) | 2.25–3.85 | 2.05–3.50 | 2.10–4.01 |
Refinement | Composite focused maps | ||
Initial model used (PDB code) | |||
Model resolution (Å) | 2.41 | ||
FSC threshold | 0.143 | ||
CC (mask) | 0.8246 | ||
Map sharpening B factor (Å2) | −73.4 | −60.5 | −62.4 |
Model composition | |||
Nonhydrogen atoms | 17,802 | ||
Protein residues | 2159 | ||
Ligands | 3 (m7GpppA, GTP, Mg) | ||
Waters | 32 | ||
B factors (Å2) | |||
Protein | 54.05 | ||
Ligand | 39.30 | ||
Waters | 39.70 | ||
R.m.s. deviations | |||
Bond lengths (Å) | 0.002 | ||
Bond angles (°) | 0.428 | ||
Validation | |||
MolProbity score | 1.38 | ||
Clashscore | 3.30 | ||
Poor rotamers (%) | 2.19 | ||
Ramachandran plot | |||
Favored (%) | 98.09 | ||
Allowed (%) | 1.91 | ||
Disallowed (%) | 0.00 | ||
