3DAL
Methyltransferase domain of human PR domain-containing protein 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 298 |
| Wavelength(s) | 1.28268 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 64.834, 64.960, 112.663 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.650 |
| R-factor | 0.197 |
| Rwork | 0.196 |
| R-free | 0.21700 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.571 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASES |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.680 |
| High resolution limit [Å] | 1.650 | 4.480 | 1.650 |
| Rmerge | 0.061 | 0.030 | 0.664 |
| Number of reflections | 57924 | ||
| <I/σ(I)> | 10.5 | ||
| Completeness [%] | 99.8 | 99 | 98.5 |
| Redundancy | 6.1 | 6.1 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | Purified PRDM1 was crystallized using hanging drop vapor diffusion method at 20 C by mixing 1.5 l of the protein solution with 1.5 l of the reservoir solution containing 2.0 M Na Formide, 0.1 M sodium acetate, pH 4.6., VAPOR DIFFUSION, HANGING DROP, temperature 293K |
