5FUL
Crystal Structure of Mus musculus Protein Arginine Methyltransferase 2 with SAH
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-07-09 |
| Detector | DECTRIS PILATUS 2M |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 65.507, 115.414, 132.963 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.260 - 1.890 |
| R-factor | 0.167 |
| Rwork | 0.166 |
| R-free | 0.19240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5fub |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.289 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.600 | 1.960 |
| High resolution limit [Å] | 1.890 | 1.890 |
| Rmerge | 0.090 | |
| Number of reflections | 40535 | |
| <I/σ(I)> | 14.9 | 1.2 |
| Completeness [%] | 99.9 | 98 |
| Redundancy | 9.2 | 8.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | 16% PEG6000, 100MM CACL2, 100MM HEPES PH7.0 |
