2RFI
Crystal structure of catalytic domain of human euchromatic histone methyltransferase 1 in complex with SAH and dimethylated H3K9 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-12-10 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.00000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 84.593, 85.627, 95.670 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.800 - 1.590 |
R-factor | 0.19403 |
Rwork | 0.193 |
R-free | 0.22014 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2igq |
RMSD bond length | 0.009 |
RMSD bond angle | 1.171 |
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] | 42.800 |
High resolution limit [Å] | 1.590 |
Rmerge | 0.080 |
Number of reflections | 89676 |
<I/σ(I)> | 10.8 |
Completeness [%] | 96.5 |
Redundancy | 7.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 300 | 16% PEG 4000, 10% Isopropanol, 0.1M Bicine pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 300K |