6GE3
X-ray structure of TEAD4 (wildtype) complexed with YAP (wildtype): The role of residual flexibility and water molecules in the adaptation of a bound intrinsically disordered protein to mutations at a binding interface
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-03-16 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.99984 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 59.149, 59.149, 158.999 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.960 - 1.850 |
| R-factor | 0.2193 |
| Rwork | 0.218 |
| R-free | 0.24210 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.066 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.960 | 1.900 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.068 | 0.704 |
| Rmeas | 0.070 | 0.733 |
| Rpim | 0.072 | 0.462 |
| Total number of observations | 321014 | |
| Number of reflections | 25036 | |
| <I/σ(I)> | 26.3 | 3.6 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 12.8 | 12.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | 16% PEG 3350,2% tacsimate, 0.1M NaCit, pH 5.6 |
