2QPW
Methyltransferase domain of human PR domain-containing protein 2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE A1 |
| Synchrotron site | CHESS |
| Beamline | A1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-06-24 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.97770 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 36.462, 51.196, 70.887 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.490 - 1.790 |
| R-factor | 0.17104 |
| Rwork | 0.168 |
| R-free | 0.22157 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Obtained via Se-SAD from second crystal (different crystal form) at low resolution |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.507 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.790 | 1.790 |
| Number of reflections | 23999 | |
| <I/σ(I)> | 34.3 | 6 |
| Completeness [%] | 99.7 | 99.3 |
| Redundancy | 7.2 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 22% PEG 5000 MME, 0.2 M Ammonium sulfate, 0.1 M MES pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
