5UVT
BRD4_BD2_A-1454056
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 | 2012-10-24 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 63.497, 70.407, 33.633 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.200 - 1.670 |
R-factor | 0.168 |
Rwork | 0.167 |
R-free | 0.19300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Apo BRD4_BD2 |
RMSD bond length | 0.010 |
RMSD bond angle | 0.920 |
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] | 35.200 |
High resolution limit [Å] | 1.670 |
Rmerge | 0.070 |
Number of reflections | 18056 |
<I/σ(I)> | 18.9 |
Completeness [%] | 100.0 |
Redundancy | 6.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 277 | Protein Buffer : 10 mM HEPES PH 7.5 100 mM NaCl 5 mM DTT Crystallization : 15 % (v/v) Ethanol Tris PH 7.0 |