Table 1 Statistics of cryoEM data collection, refinement, and validation.
From: CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
HnRNPA2-LCD (EMD-21871) (PDB: 6WQK) | |
|---|---|
Data collection and processing | |
Magnification | ×130,000 |
Voltage (kV) | 300 |
Electron exposure (e– Å−2) | 34.5 |
Defocus range (μm) | 0.8–5.1 |
Pixel size (Å) | 1.064 |
Symmetry imposed | C1; Helical |
Initial particle images (no.) | 529,821 |
Final particle images (no.) | 132,571 |
Map resolution (Å) | 3.1 |
FSC threshold | 0.143 |
Map resolution range (Å) | 200–3.1 |
Refinement | |
Initial model used | De Novo |
Model resolution (Å) | 3.2 |
FSC threshold | 0.5 |
Model resolution range (Å) | 200–3.2 |
Map sharpening B factor (Å2) | −120 |
Model composition | |
Non-hydrogen atoms | 2070 |
Protein residues | 285 |
B factors (Å2) | |
Protein | 55.3 |
R.m.s. deviations | |
Bond lengths (Å) | 0.006 |
Bond angles (°) | 0.89 |
Validation | |
MolProbity score | 1.70 |
Clashscore | 5.59 |
Poor rotamers (%) | 0.00 |
Ramachandran plot | |
Favored (%) | 94 |
Allowed (%) | 6 |
Disallowed (%) | 0.00 |
