4JUY
Crystal structure of the PUB domain of E3 ubiquitin ligase RNF31
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-02-11 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97926 |
Spacegroup name | F 4 3 2 |
Unit cell lengths | 256.488, 256.488, 256.488 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.410 - 2.400 |
R-factor | 0.237 |
Rwork | 0.236 |
R-free | 0.25820 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.256 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | SOLVE (2.13) |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.440 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.072 | 0.973 |
Number of reflections | 28765 | |
<I/σ(I)> | 43.6 | 3 |
Completeness [%] | 100.0 | 100 |
Redundancy | 14.2 | 14.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 291 | 0.8M K/Na tartrate tetrahydrate, 0.5% PEG MME 5000, 0.1 M BisTris, pH 8.5, vapor diffusion, hanging drop, temperature 291K |