5FWA
Crystal Structure of Mus musculus Protein Arginine Methyltransferase 2 with CP1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-04-25 |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 66.183, 114.676, 132.653 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.369 - 1.800 |
R-factor | 0.1727 |
Rwork | 0.172 |
R-free | 0.19070 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5fub |
RMSD bond length | 0.006 |
RMSD bond angle | 0.854 |
Data reduction software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.200 | 1.840 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.090 | |
Number of reflections | 47105 | |
<I/σ(I)> | 11.7 | 1 |
Completeness [%] | 100.0 | 100 |
Redundancy | 6.5 | 6.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 24% PEG6000, 100 MM HEPES PH7, 100MM CACL2 |