Table 1 Data collection and refinement statistics for importin α1 structures
From: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses
Impα1a | NiV W Impα1a | HeV W Impα1a | |
|---|---|---|---|
Data Collection | |||
Wavelength (Å) | 0.9537 | 0.9537 | 0.9537 |
Space group | P 21 21 21 | P 21 21 21 | P 21 21 21 |
Cell dimensions | |||
a, b, c (Å) | 78.5, 90.0, 100.7 | 77.9, 88.8, 97.6 | 79.0, 89.3, 100.4 |
α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | 90, 90, 90 |
Resolution (Å) | 24.54–2.50 (2.60–2.50) | 29.61–2.10 (2.16–2.10) | 19.76–2.20 (2.28–2.20) |
Rpim | 0.061 (0.365) | 0.033 (0.253) | 0.029 (0.147) |
Mean I/σ (I) | 10.2 (2.9) | 11.7 (2.4) | 18.5 (5.4) |
CC1/2 | 0.989 (0.751) | 0.998 (0.814) | 0.999 (0.928) |
Total reflections | 154,003 (17460) | 136,253 (11369) | 208,967 (18156) |
Unique reflections | 24,805 (2822) | 38,272 (3193) | 36,721 (3139) |
Completeness (%) | 98.6 (100) | 96 (97.8) | 99.8 (100) |
Redundancy | 6.2 (6.2) | 3.6 (3.6) | 5.7 (5.8) |
Wilson B-factor | 26.4 | 31.8 | 22.6 |
Refinement | |||
Resolution (Å) | 24.54–2.50 | 28.79–2.10 | 19.76–2.20 |
Reflections used in | |||
Refinement | 24,772 (2478) | 38,216 (3843) | 36,662 (3611) |
Rfree | 1262 (133) | 1864 (172) | 1861 (176) |
Rwork | 0.1910 (0.2227) | 0.1854 (0.2690) | 0.1915 (0.2257) |
Rfree | 0.2129 (0.2572) | 0.2032 (0.3062) | 0.2121 (0.2774) |
Number of non-hydrogen atoms | 3361 | 3555 | 3431 |
Macromolecules | 3244 | 3306 | 3306 |
Protein residues | 426 | 434 | 434 |
B factors | 42.49 | 51.14 | 38.89 |
Protein | 42.66 | 51.31 | 38.98 |
Water | 37.95 | 48.89 | 36.67 |
R.M.S. deviations | |||
Bond lengths (Å) | 0.004 | 0.005 | 0.003 |
Bond angles (°) | 0.59 | 0.73 | 0.62 |
Ramachandran plot (%) | |||
Favoured | 99 | 99 | 98 |
Allowed | 1.4 | 1.4 | 1.9 |
Outliers | 0 | 0 | 0 |
Rotamer outliers (%) | 1.1 | 1.1 | 0.27 |
Clash score | 0.46 | 0.90 | 1.19 |
