6GYR
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 | 2013-11-17 |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 1.282 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 100.826, 146.717, 116.477 |
Unit cell angles | 90.00, 91.75, 90.00 |
Refinement procedure
Resolution | 50.000 - 3.100 |
R-factor | 0.2113 |
Rwork | 0.209 |
R-free | 0.26460 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4bhw |
RMSD bond length | 0.008 |
RMSD bond angle | 1.242 |
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] | 50.000 | 3.250 |
High resolution limit [Å] | 3.100 | 3.100 |
Number of reflections | 106462 | |
<I/σ(I)> | 7.48 | |
Completeness [%] | 99.0 | |
Redundancy | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 277 | 100 mM HEPES, pH 7.5, 18-22% polyethylene glycol 3350, 0.2 M NaCl |