4QBR
Crystal structure of DNMT3a ADD domain G550D mutant bound to H3 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U |
| Synchrotron site | SSRF |
| Beamline | BL17U |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-04-17 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 1 |
| Unit cell lengths | 36.057, 37.161, 50.125 |
| Unit cell angles | 78.70, 83.89, 81.56 |
Refinement procedure
| Resolution | 36.136 - 1.902 |
| R-factor | 0.1802 |
| Rwork | 0.178 |
| R-free | 0.22520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.093 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 5.160 | 1.900 |
| Number of reflections | 19077 | ||
| Completeness [%] | 96.7 | 99.2 | 96 |
| Redundancy | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 291 | 25% PEG3350, 0.1M Bis-Tris-HCL, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
