3QII
Crystal structure of tudor domain 2 of human PHD finger protein 20
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-09-22 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97911 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 48.683, 48.683, 96.273 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.300 |
| R-factor | 0.237 |
| Rwork | 0.235 |
| R-free | 0.26800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o4x |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.361 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 6.240 | 2.300 |
| Rmerge | 0.069 | 0.030 | 0.318 |
| Number of reflections | 5606 | ||
| <I/σ(I)> | 12.8 | ||
| Completeness [%] | 99.2 | 99.1 | 86.8 |
| Redundancy | 12.3 | 11.2 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | 25% PEG-8000, 0.2M sodium chloride, 0.1M TRIS, pH 8.5, vapor diffusion, sitting drop, temperature 291K |






