4C07
Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with CaCl2 at 1.5 Angstroms
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 | 2012-07-13 |
| Detector | MARRERESEARCH |
| Spacegroup name | I 41 |
| Unit cell lengths | 79.740, 79.740, 118.572 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.857 - 1.499 |
| R-factor | 0.1421 |
| Rwork | 0.133 |
| R-free | 0.15730 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2y1w |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.264 |
| 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] | 40.860 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.080 | 1.170 |
| Number of reflections | 58495 | |
| <I/σ(I)> | 13.59 | 0.84 |
| Completeness [%] | 98.9 | 90.1 |
| Redundancy | 6.8 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 100 MM HEPES PH 8.0, 200 MM CACL2, 12% PEG 6000 |
