Table 1 Data collection and structure refinement statistics of PML B1-box
From: B1 oligomerization regulates PML nuclear body biogenesis and leukemogenesis
Protein | PML B1-box |
|---|---|
Data collection | |
Space group | P21 |
Unit cell (Å, °) | |
a, b, c | 36.7, 50.5, 51.4 |
β | 101.4 |
Molecule per ASU | 4 |
Derivative | Native |
Source/stationa | BL17U |
Wavelength (Å) | 1.282 |
Resolution range (Å) | 50.4–2.06 |
Observations (Ι/σ(Ι) > 0) | 45412 |
Unique reflections (Ι/σ(Ι) > 0) | 11287 (1650) |
High resolution shell (Å) | 2.17–2.06 |
Rsym (%)b,c | 17.7 (69.4) |
< Ι/σ(Ι) > c | 5.5 (2.9) |
Completenessc (%) | 98.0 (98.3) |
Redundancyc | 4.0 (4.1) |
CC1/2 | 0.97 (0.61) |
Structure refinement | |
Resolution range (Å) | 25.2–2.06 |
R-factor (%) | 18.6 |
R-factor (high resolution shell)d | 24.6 |
Rfree (%)e | 22.7 |
Rfree (high resolution shell) | 27.7 |
Total number of non-hydrogen atoms | 1700 |
Protein atoms | 1609 |
Water molecules | 82 |
R.m.s. deviationsf | |
Bond length (Å) | 0.006 |
Bond angle (°) | 0.993 |
Wilson B-factor (Å2) | 25.9 |
Average B-factor protein atoms (Å2) | 40.3 |
Average B-factor water atoms (Å2) | 45.5 |
Ramachandran statistics (%) | |
Most favored region | 97.4 |
Allowed regions | 2.6 |
Outliers | 0 |
