5UVS
BRD4_BD2_A-1406537
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-02-29 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 56.926, 73.535, 33.617 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.770 - 2.150 |
R-factor | 0.209 |
Rwork | 0.207 |
R-free | 0.24700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Apo-BRD4_BD2 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.000 |
Data reduction software | XDS (2.11.7) |
Data scaling software | SCALA |
Refinement software | BUSTER (2.11.7) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 36.800 |
High resolution limit [Å] | 2.150 |
Rmerge | 0.085 |
Number of reflections | 8099 |
<I/σ(I)> | 14.4 |
Completeness [%] | 100.0 |
Redundancy | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 277 | Protein Buffer : 10 mM HEPES PH 7.5 100 mM NaCl 5mM DTT Crystallization : 15 % (v/v) Ethanol Tris PH 7.0 |