5UF0
BRD4_BD2-A-35165
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 | 2010-08-09 |
Detector | DECTRIS PILATUS 300K |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 57.049, 73.030, 33.596 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.510 - 1.350 |
R-factor | 0.18 |
Rwork | 0.179 |
R-free | 0.20100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Apo-BRD4_BD2 |
RMSD bond length | 0.010 |
RMSD bond angle | 0.960 |
Data reduction software | XDS (2.11.7) |
Data scaling software | SCALA (3.20) |
Refinement software | BUSTER-TNT |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 73.000 |
High resolution limit [Å] | 1.350 |
Number of reflections | 31000 |
<I/σ(I)> | 19.4 |
Completeness [%] | 98.0 |
Redundancy | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7 | 277 | Protein buffer : PH 7.5 10 mM HEPES 100 mM NaCl 5mM DTT Crystallization : 15 %(V/V) Ethanol Tris PH 7.0 |