6PDM
Crystal structure of Human Protein Arginine Methyltransferase 9 (PRMT9)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-02-21 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 64.812, 83.802, 65.711 |
| Unit cell angles | 90.00, 98.16, 90.00 |
Refinement procedure
| Resolution | 65.000 - 2.450 |
| R-factor | 0.219 |
| Rwork | 0.216 |
| R-free | 0.26000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PHENIX.MR_ROSETTA with PDB entry 4C4A |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.190 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | MR-Rosetta |
| Refinement software | BUSTER (2.10.2) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 65.050 | 65.050 | 2.490 |
| High resolution limit [Å] | 2.400 | 8.970 | 2.400 |
| Rmerge | 0.072 | 0.022 | 1.208 |
| Rmeas | 0.085 | 0.026 | 1.419 |
| Rpim | 0.045 | 0.014 | 0.739 |
| Total number of observations | 92810 | 1846 | 9728 |
| Number of reflections | 27005 | 551 | 2704 |
| <I/σ(I)> | 11 | 45.5 | 0.9 |
| Completeness [%] | 98.7 | 99.6 | 94.7 |
| Redundancy | 3.4 | 3.4 | 3.6 |
| CC(1/2) | 0.998 | 0.999 | 0.468 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 293 | 20% PEG3350, 0.2M ammonium nitrate |
