1R1S
Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-04-20 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.637, 117.937, 50.594 |
| Unit cell angles | 90.00, 108.92, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| R-factor | 0.21745 |
| Rwork | 0.213 |
| R-free | 0.25855 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.037 |
| RMSD bond angle | 2.883 |
| Data reduction software | CrystalClear ((MSC/RIGAKU)) |
| Data scaling software | d*TREK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 52.300 |
| High resolution limit [Å] | 1.840 |
| Number of reflections | 41324 |
| Completeness [%] | 92.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 8.5 | 298 | 0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.5, VAPOR DIFFUSION, temperature 298K |
