3DB4
Crystal structure of the tandem tudor domains of the E3 ubiquitin-protein ligase UHRF1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-03-05 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 62 |
| Unit cell lengths | 98.654, 98.654, 43.345 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 38.660 - 2.400 |
| R-factor | 0.22008 |
| Rwork | 0.217 |
| R-free | 0.28462 |
| Structure solution method | SAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.055 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.660 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Number of reflections | 9579 | |
| <I/σ(I)> | 25.55 | 4.76 |
| Completeness [%] | 99.7 | 97.4 |
| Redundancy | 11.9 | 10.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 10 % PEG 8000, 0.1 M SODIUM CACODYLATE, 0.2 M AMMONIUM SULFATE, 0.001 M TCEP, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
