4I51
Methyltransferase domain of HUMAN EUCHROMATIC HISTONE METHYLTRANSFERASE 1, mutant Y1211A
Replaces: 4H4HExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-03-11 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97958 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 83.497, 83.800, 95.052 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.780 - 1.900 |
| R-factor | 0.171 |
| Rwork | 0.171 |
| R-free | 0.19500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3hna |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.163 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0027) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.072 | 0.561 |
| Number of reflections | 52417 | |
| <I/σ(I)> | 10.5 | |
| Completeness [%] | 98.6 | 83 |
| Redundancy | 7.9 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 10% ISOPROPANOL, 20% PEG4000; 0.1M HEPES PH7.5, VAPOR DIFFUSION HANGING DROP, TEMPERATURE 297K |






