4C06
Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with MgCl2
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 | CCD |
| Collection date | 2012-07-22 |
| Detector | MARRESEARCH |
| Spacegroup name | I 41 |
| Unit cell lengths | 79.758, 79.758, 118.945 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.923 - 1.600 |
| R-factor | 0.1573 |
| Rwork | 0.155 |
| R-free | 0.19390 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2y1w |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.279 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.920 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.080 | |
| Number of reflections | 48039 | |
| <I/σ(I)> | 17.29 | 0.9 |
| Completeness [%] | 98.4 | 86.5 |
| Redundancy | 8.2 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | pH 8.0 |
