3HNA
Crystal structure of catalytic domain of human euchromatic histone methyltransferase 1 in complex with SAH and mono-Methylated H3K9 Peptide
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 | 2007-01-01 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 83.526, 83.372, 95.130 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 62.750 - 1.500 |
R-factor | 0.16738 |
Rwork | 0.166 |
R-free | 0.19273 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2rfi |
RMSD bond length | 0.009 |
RMSD bond angle | 1.285 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 100.000 |
High resolution limit [Å] | 1.500 |
Rmerge | 0.070 |
Number of reflections | 101405 |
<I/σ(I)> | 12 |
Completeness [%] | 96.5 |
Redundancy | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 300 | 20%PEG3350, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 300K |