3MEA
Crystal structure of the SGF29 in complex with H3K4me3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-15 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97927 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 93.385, 41.425, 52.527 |
| Unit cell angles | 90.00, 121.39, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.260 |
| R-factor | 0.179 |
| Rwork | 0.178 |
| R-free | 0.20000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3me9 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.537 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 1.280 |
| High resolution limit [Å] | 1.260 | 3.420 | 1.260 |
| Rmerge | 0.052 | 0.018 | 0.973 |
| Number of reflections | 46388 | ||
| <I/σ(I)> | 9.8 | ||
| Completeness [%] | 99.9 | 99.4 | 99.1 |
| Redundancy | 3.5 | 3.7 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 22% peg3350, 0.1M HEPES. 0.004M trimethylated H3K3 peptide was present in the protein stock solution, pH 7.5, vapor diffusion, hanging drop, temperature 291K |
