8PJD
Crystal Structure of Mus musculus Protein Arginine Methyltransferase 2 94-445
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-05-04 |
| Detector | DECTRIS EIGER R 4M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 65.052, 115.980, 133.718 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.250 - 1.600 |
| R-factor | 0.1723 |
| Rwork | 0.171 |
| R-free | 0.18910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.005 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.21rc1_4958: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.250 | 1.630 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.075 | 2.384 |
| Rmeas | 0.078 | 2.527 |
| Rpim | 0.021 | 0.808 |
| Number of reflections | 65279 | 2584 |
| <I/σ(I)> | 17.7 | 0.8 |
| Completeness [%] | 97.5 | 77.85 |
| Redundancy | 7 | 9.2 |
| CC(1/2) | 0.999 | 0.380 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.3 | 293 | 1.3M AcONa pH5.3 |






