1ORI
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 | 2000-03-31 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 41 2 2 |
| Unit cell lengths | 88.270, 88.270, 145.140 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.180 - 2.500 |
| Rwork | 0.199 |
| R-free | 0.26300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f3l |
| RMSD bond length | 0.008 |
| 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 | 2.540 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.100 | 0.213 |
| Total number of observations | 102483 * | |
| Number of reflections | 20200 | |
| <I/σ(I)> | 19.2 | 6.7 |
| Completeness [%] | 98.6 | 96.2 |
| Redundancy | 5.07 |
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 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | reservoir | Tris | 100 (mM) | pH9.0 |
| 3 | 1 | reservoir | ammonium phosphate monobasic | 1.6 (M) | pH4.7 |
