3IIW
Crystal structure of Eed in complex with a trimethylated histone H3K27 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9700 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 57.745, 85.118, 91.246 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.800 |
R-factor | 0.15896 |
Rwork | 0.157 |
R-free | 0.19315 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | SeMet Eed structure |
RMSD bond length | 0.010 |
RMSD bond angle | 1.486 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.880 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.073 | 0.279 |
Number of reflections | 40269 | |
<I/σ(I)> | 11.3 | 2.8 |
Completeness [%] | 97.8 | 85.8 |
Redundancy | 3.7 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 4.0 M Sodium formate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |