6L9F
Crystal structure of TEAD4 in complex with a novel FAM181A peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U1 |
| Synchrotron site | SSRF |
| Beamline | BL17U1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-10-04 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.00928 |
| Spacegroup name | P 64 2 2 |
| Unit cell lengths | 110.009, 110.009, 182.711 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 46.094 - 2.555 |
| R-factor | 0.1959 |
| Rwork | 0.190 |
| R-free | 0.25280 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3jua |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.970 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.590 |
| High resolution limit [Å] | 2.550 | 6.920 | 2.550 |
| Rmerge | 0.185 | 0.052 | 0.901 |
| Rmeas | 0.191 | 0.054 | 0.933 |
| Rpim | 0.050 | 0.015 | 0.239 |
| Total number of observations | 320535 | ||
| Number of reflections | 21907 | 1233 | 1064 |
| <I/σ(I)> | 6.3 | ||
| Completeness [%] | 99.8 | 97.8 | 100 |
| Redundancy | 14.6 | 13 | 15 |
| CC(1/2) | 0.999 | 0.907 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 289 | 2.5 M Ammonium nitrate, 0.1 M Sodium acetate trihydrate pH 4.6 |
