5EMV
Crystal structure of the palmitoylated human TEAD2 transcription factor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-08-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9787 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 79.830, 61.250, 112.672 |
| Unit cell angles | 90.00, 101.89, 90.00 |
Refinement procedure
| Resolution | 53.543 - 2.000 |
| R-factor | 0.2034 |
| Rwork | 0.202 |
| R-free | 0.23130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3l15 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.668 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (0.5.4) |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 58.320 | 58.320 | 2.050 |
| High resolution limit [Å] | 2.000 | 8.940 | 2.000 |
| Rmerge | 0.072 | 0.024 | 0.674 |
| Rpim | 0.043 | 0.016 | 0.405 |
| Total number of observations | 137128 | 1474 | 10185 |
| Number of reflections | 36163 | ||
| <I/σ(I)> | 9.9 | 26.2 | 2 |
| Completeness [%] | 100.0 | 98.7 | 100 |
| Redundancy | 3.8 | 3.4 | 3.8 |
| CC(1/2) | 0.998 | 0.996 | 0.812 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.3 | 292 | 1.7-2.1 M Sodium Formate |






