3UA4
Crystal Structure of Protein Arginine Methyltransferase PRMT5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-06-20 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 100.560, 129.490, 149.719 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.024 - 3.005 |
| R-factor | 0.2346 |
| Rwork | 0.232 |
| R-free | 0.28850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ua3 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.858 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: 1.6.2_432)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.024 | 3.110 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.074 | 0.487 |
| Number of reflections | 39417 | |
| <I/σ(I)> | 20.2 | 3 |
| Completeness [%] | 99.7 | 99.9 |
| Redundancy | 4.8 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 289 | 100mM Tris, 9% PEG-5000MME, 5% Tacsimate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
