1ORH
Structure of the Predominant Protein Arginine Methyltransferase PRMT1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X26C |
| Synchrotron site | NSLS |
| Beamline | X26C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-04-02 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 41 2 2 |
| Unit cell lengths | 87.840, 87.840, 144.570 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.640 |
| Rwork | 0.186 |
| R-free | 0.24800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f3l |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.730 |
| High resolution limit [Å] | 2.640 | 2.640 |
| Rmerge | 0.084 | 0.297 |
| Number of reflections | 17213 | |
| <I/σ(I)> | 20.8 | 6.3 |
| Completeness [%] | 99.8 | 99.3 |
| Redundancy | 6.76 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.7 | 289 | ammonium phosphate, pH 4.7, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
