1H3I
Crystal structure of the Histone Methyltransferase SET7/9
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Wavelength(s) | 0.9794, 0.9394, 0.9800 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 66.090, 82.830, 116.150 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 * - 2.100 |
| R-factor | 0.212 |
| Rwork | 0.210 |
| R-free | 0.25800 * |
| Structure solution method | MAD |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.500 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 30.000 * |
| High resolution limit [Å] | 2.100 |
| Rmerge | 0.048 * |
| Number of reflections | 37053 |
| Completeness [%] | 84.0 * |
| Redundancy | 3.1 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7 | pH 7.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris | 50 (mM) | pH7.0 |
| 3 | 1 | drop | 100 (mM) | ||
| 4 | 1 | drop | TCEP | 1 (mM) | |
| 5 | 1 | reservoir | magnesium formate | 0.2 (M) | |
| 6 | 1 | reservoir | PEG3350 | 25 (%) |
