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 (%) |