3DB3
Crystal structure of the tandem tudor domains of the E3 ubiquitin-protein ligase UHRF1 in complex with trimethylated histone H3-K9 peptide
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 | 2008-04-09 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.99987 |
| Spacegroup name | P 62 |
| Unit cell lengths | 99.622, 99.622, 41.232 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 31.770 - 2.400 |
| R-factor | 0.21512 |
| Rwork | 0.212 |
| R-free | 0.28198 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.298 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | REFMAC (5.2.0019) |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Number of reflections | 9214 | |
| <I/σ(I)> | 22.52 | 3.62 |
| Completeness [%] | 98.8 | 92.9 |
| Redundancy | 6.9 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 298 | 3 M SODIUM FORMATE, 0.1 M SODIUM ACETATE, pH 5.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
