2YYR
Structural analysis of PHD domain of Pygopus complexed with trimethylated histone H3 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-5A |
Synchrotron site | Photon Factory |
Beamline | BL-5A |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 59.518, 59.518, 95.853 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.430 - 2.500 |
R-factor | 0.213 |
Rwork | 0.213 |
R-free | 0.23400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2dx8 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.094 | 0.315 |
Number of reflections | 6470 | |
Completeness [%] | 99.8 | 100 |
Redundancy | 13.9 | 13.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | co-crystallization | 9 | 298 | 1.0M Na Citrate, 0.1M LiSo4, 0.1mM ZnCl2, 50mM Tris-HCl, pH 9.0, co-crystallization, temperature 298K |