3SMQ
Crystal structure of protein arginine methyltransferase 3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08ID-1 |
| Synchrotron site | CLSI |
| Beamline | 08ID-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-05-25 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97949 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 70.649, 70.649, 171.977 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.000 |
| R-factor | 0.19065 |
| Rwork | 0.190 |
| R-free | 0.21534 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fyt |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.214 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.078 | 0.558 |
| Number of reflections | 29893 | |
| <I/σ(I)> | 36.6 | 2.2 |
| Completeness [%] | 98.8 | 83.4 |
| Redundancy | 11.5 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 297 | 20.0% PEG 4K, 0.2M Mg OAc, 0.1M Na CaCo pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K |
