3FL2
Crystal structure of the ring domain of the E3 ubiquitin-protein ligase UHRF1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2008-12-11 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.54178 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.736, 46.916, 48.409 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.750 |
| R-factor | 0.18654 |
| Rwork | 0.183 |
| R-free | 0.24976 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1z6u |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.500 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0063) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Number of reflections | 11019 | |
| <I/σ(I)> | 43.78 | 10.761 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 5.2 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 27% PEG MME 2000, 0.1 M TRIS-HCL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
