6FNX
FIRST DOMAIN OF HUMAN BROMODOMAIN BRD4 IN COMPLEX WITH INHIBITOR F1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE MASSIF-1 |
Synchrotron site | ESRF |
Beamline | MASSIF-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-02-12 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 0.966 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 37.863, 44.175, 78.156 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.080 - 1.190 |
R-factor | 0.23407 |
Rwork | 0.232 |
R-free | 0.27634 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2oss |
RMSD bond length | 0.034 |
RMSD bond angle | 2.840 |
Data reduction software | XDS (0.53) |
Data scaling software | XDS (0.53) |
Phasing software | PHASER (2.6.1) |
Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.080 | 1.230 |
High resolution limit [Å] | 1.190 | 1.190 |
Rmerge | 0.102 | 0.772 |
Rmeas | 0.116 | 0.880 |
Rpim | 0.053 | 0.414 |
Number of reflections | 41897 | 4061 |
<I/σ(I)> | 8.27 | 1.63 |
Completeness [%] | 98.4 | 97.55 |
Redundancy | 4.5 | 4.3 |
CC(1/2) | 0.996 | 0.643 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 292 | 5mM of #F1 inhibitor (in DMSO) final concentration. Ratio 1:1 (protein:precipitant). 20mg/mL of BRD4(BD1) protein. 0.25M AmSO4; 0.1M NaCl; 0,1M Tris pH 8.5; 19% (w/v) PEG3350. Cryoprotectant: 10 % (w/v) ethylene glycol. |