6GYT
Transcription factor dimerization activates the p300 acetyltransferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-10-09 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.640, 83.710, 165.620 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.087 - 2.500 |
| R-factor | 0.2619 |
| Rwork | 0.261 |
| R-free | 0.28820 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4bhw |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.578 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.600 | 2.600 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Number of reflections | 23996 | |
| <I/σ(I)> | 7.6 | |
| Completeness [%] | 97.3 | |
| Redundancy | 9.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 294 | 1.6 M Ammonium Sulfate, 100 mM Bicine, pH 9.0 |






