1R5W
Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T-cell activation
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-12-02 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1 |
| Spacegroup name | P 41 |
| Unit cell lengths | 116.132, 116.132, 85.935 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.900 |
| R-factor | 0.291 |
| Rwork | 0.289 |
| R-free | 0.30800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 26.200 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.000 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.059 | 0.436 |
| Total number of observations | 82306 * | |
| Number of reflections | 26403 | |
| <I/σ(I)> | 21 | |
| Completeness [%] | 93.1 | 83.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 * | 298 | PEG, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | HEPES | 10 (mM) | pH7.2 |
| 3 | 1 | drop | 150 (mM) | ||
| 4 | 1 | reservoir | 2 (M) | ||
| 5 | 1 | reservoir | sodium acetate | 0.1 (M) | pH4.2 |
| 6 | 1 | reservoir | 0.1 (M) |
