1R1Q
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 | 2003-04-23 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.710, 51.810, 43.970 |
Unit cell angles | 90.00, 101.38, 90.00 |
Refinement procedure
Resolution | 43.030 - 1.800 |
R-factor | 0.17906 |
Rwork | 0.176 |
R-free | 0.22530 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.023 |
RMSD bond angle | 1.924 |
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] | 43.100 |
High resolution limit [Å] | 1.620 |
Number of reflections | 26632 |
Completeness [%] | 96.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8.7 | 298 | 0.1mM Tris-HCl, 2.5M ammonium sulfate, pH 8.7, VAPOR DIFFUSION, temperature 298K |