3QL9
Monoclinic complex structure of ATRX ADD bound to histone H3K9me3 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BSRF BEAMLINE 3W1A |
| Synchrotron site | BSRF |
| Beamline | 3W1A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-10-02 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.97924 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 83.719, 39.452, 41.057 |
| Unit cell angles | 90.00, 111.24, 90.00 |
Refinement procedure
| Resolution | 21.950 - 0.930 |
| R-factor | 0.1227 |
| Rwork | 0.122 |
| R-free | 0.13110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3qln |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.414 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 0.950 |
| High resolution limit [Å] | 0.930 | 2.520 | 0.930 |
| Rmerge | 0.067 | 0.037 | 0.570 |
| Number of reflections | 77964 | ||
| <I/σ(I)> | 8 | ||
| Completeness [%] | 93.1 | 98.8 | 88.1 |
| Redundancy | 8.5 | 8.4 | 8.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.1 | 277 | 14% PEG 4000, 0.1M MES, 0.2 M KCL, pH 6.1, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
