6ASZ
Chromodomain HP1 with Y24F mutation bound to histone H3 peptide containing trimethyl lysine
Replaces: 5KOGExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-11-09 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.000 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 34.516, 76.780, 75.508 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.894 - 1.518 |
| R-factor | 0.2561 |
| Rwork | 0.255 |
| R-free | 0.27390 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kne |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.749 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 10.894 |
| High resolution limit [Å] | 1.518 |
| Number of reflections | 15582 |
| <I/σ(I)> | 4.4 |
| Completeness [%] | 98.2 |
| Redundancy | 5.66 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.3 | 277 | 0.1 M MES, 3.4 M (NH4)2SO4 |






