4C03
Crystal structure of M. musculus protein arginine methyltransferase PRMT6 reduced
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-12-17 |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 118.722, 143.340, 41.958 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.560 - 1.580 |
R-factor | 0.1617 |
Rwork | 0.160 |
R-free | 0.19140 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2y1w |
RMSD bond length | 0.010 |
RMSD bond angle | 1.281 |
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] | 39.560 | 1.640 |
High resolution limit [Å] | 1.580 | 1.580 |
Rmerge | 0.110 | 1.010 |
Number of reflections | 98190 | |
<I/σ(I)> | 8.71 | 0.99 |
Completeness [%] | 99.0 | 90.7 |
Redundancy | 6.3 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 100 MM HEPES PH 7.0, 200 MM MGCL2, 25% PEG 1500 |