5DQE
Crystal structure of human transcription factor TEAD2 in complex with bromo-fenamic acid
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-06-13 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.91925 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 121.470, 61.582, 80.419 |
Unit cell angles | 90.00, 117.70, 90.00 |
Refinement procedure
Resolution | 38.669 - 2.183 |
R-factor | 0.1812 |
Rwork | 0.179 |
R-free | 0.22740 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3l15 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.498 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | PHENIX ((phenix.refine: dev_1951)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.220 |
High resolution limit [Å] | 2.180 | 2.180 |
Number of reflections | 24263 | |
<I/σ(I)> | 24 | 3.14 |
Completeness [%] | 98.4 | 86.6 |
Redundancy | 4 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 293 | 0.1 M HEPES pH 7.2 and 2.4 M sodium formate. |