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 |