5EMW
Crystal structure of the palmitoylated human TEAD3 transcription factor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-07-29 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9795 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.310, 123.530, 150.730 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 95.540 - 2.550 |
R-factor | 0.186 |
Rwork | 0.184 |
R-free | 0.22300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5emv |
RMSD bond length | 0.003 |
RMSD bond angle | 0.674 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (0.5.9) |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 95.540 | 2.660 |
High resolution limit [Å] | 2.550 | 2.550 |
Rmerge | 0.118 | 0.691 |
Number of reflections | 38149 | |
<I/σ(I)> | 9.5 | 2.5 |
Completeness [%] | 94.9 | 96.8 |
Redundancy | 5 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 292 | 100 mM Sodium Acetate, 100 mM Calcium acetate, 12% PEG4000 |