5K8V
Crystal Structure of Mus musculus Protein Arginine Methyltransferase 4 (CARM1 130-487) with CP1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 2 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-03-26 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9801 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 75.084, 98.094, 206.260 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.716 - 2.250 |
| R-factor | 0.1945 |
| Rwork | 0.192 |
| R-free | 0.23480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5ih3 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.477 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((dev_2386: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.720 | 2.300 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.282 | 2.132 |
| Number of reflections | 73068 | |
| <I/σ(I)> | 5.7 | 1.1 |
| Completeness [%] | 99.8 | 97.6 |
| Redundancy | 6.5 | 6.6 |
| CC(1/2) | 0.986 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | Tris-HCl pH 8.0 100 mM, PEG 2000 MME 15 %, NaCl 100 mM |






