Table 1 Data collection, scaling and refinement statistics
From: The crystal structure of the Hazara virus nucleocapsid protein
Dataset | Apo-HAZV N |
|---|---|
Wavelength (Ã…) | (i02) 0.9795 |
Space group | P212121 |
Cell parameters (Å,°) | a = 64.99; b = 76.10; c = 449.30 α = 90; β = 90; γ = 90 |
Total reflections | 252499 (17368) |
Unique reflections | 62009 (4410) |
Resolution shells (Ã…) | |
Low | 74.88–2.70 |
High | 2.77–2.70 |
R merge, % | 11.6 (63.1) |
Rpim % | 8.6 (50.8) |
Completeness, % | 98.9 (98.2) |
Multiplicity | 4.1 (3.9) |
I/σ(I) | 9.3 (1.7) |
Rcryst % | 24.18 |
Rfree % | 28.12 |
VM | 2.57 |
Mol. Per AU | 4 |
Reflections working set | 58670 |
Free R-value set (no. of reflections) | 5.1 % (3125) |
RMSD bond lengths (Ã…) | 0.013 |
RMSD bond angles (°) | 1.553 |
No. atoms used in refinement | |
Non-hydrogen atoms | 15226 |
Protein atoms | 15156 |
Water molecules | 70 |
RNA atoms | 0 |
Mean B factor, Ã…2 | |
Total | 44.90 |
Protein atoms | 44.7 |
Water molecules | 51.1 |
Ramachandran plot statistics, % | |
Preferred region | 96.49 |
Allowed region | 2.88 |
Outliers | 0.27 |
Molprobity clashscore for all atoms | 2.85 |