3F2K
Structure of the transposase domain of human Histone-lysine N-methyltransferase SETMAR
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E DW |
| Temperature [K] | 200 |
| Wavelength(s) | 1.504 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 158.826, 46.521, 61.748 |
| Unit cell angles | 90.00, 92.04, 90.00 |
Refinement procedure
| Resolution | 79.310 - 1.850 |
| R-factor | 0.20764 |
| Rwork | 0.205 |
| R-free | 0.25617 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2f7t |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.729 |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.850 |
| Number of reflections | 36815 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | Purified SETMAR transposase domain was crystallized in 20% PEG 3350, 0.2 M di-Na Tartrate., pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
