Table 1.
Data collection and structure refinement statistics of PML-RING
| Data collection | |
|---|---|
| Space group | P212121 |
| Unit cell dimension (Å) | |
| a | 38.5 |
| b | 84.7 |
| c | 86.1 |
| Molecule per ASU | 4 |
| Derivative | Native |
| Source/Stationa | BL17U |
| Wavelength (Å) | 1.2824, Znpeak |
| Resolution range (Å) | 60.4 - 1.60 |
| Observations (I/σ(I) > 0) | 467248 |
| Unique reflections (I/σ(I) > 0) | 37754 |
| High resolution shell (Å) | 1.69-1.60 |
| Rsym (%)b,c | 14.9 (133.6) < I/σ(I) > c: 8.0 (1.3) |
| Completenessc (%) | 99.4 (99.9) |
| Redundancyc | 2.4 (11.5) |
| CC1/2 | 0.996 (0.848) |
| Structure refinement | |
| Resolution range (Å) | 60.4 - 1.60 |
| R-factor (%) | 20.3 |
| R-factor (high resolution shell)d | 35.0 |
| Rfree (%)e | 21.7 |
| Rfree (high resolution shell) | 36.6 |
| Total number of non-hydrogen atoms | |
| Protein atoms | 1403 |
| Water molecules | 224 |
| Zn ions | 8 |
| R.m.s. deviationsf | |
| Bond length (Å) | 0.005 |
| Bond angle (°) | 0.954 |
| Main chain B-factors (Å2) | 1.799 |
| Side chain B-factors (Å2) | 5.871 |
| Wilson B-factor (Å2) | 22.1 |
| Average B-factor (Å2) | |
| Protein atoms | 43.8 |
| Solvent atoms | 49.5 |
| Zn ions | 38.3 |
| Ramachandran statistics (%) | |
| Most favored region | 99.4 |
| Allowed regions | 0.6 |
aBeamline designations refer to the Shanghai Synchrotron Radiation Facility, Shanghai, P. R. of China
bRsym = Σ(I − <I>)2/ΣI2
coverall, high resolution shell in parentheses
dhigh resolution shell: 1.640–1.600 Å
eRfree calculated using 5% of total reflections omitted from refinement
fR.m.s. deviations report root mean square deviations from ideal bond lengths/angles and of B-factors between bonded atoms44