3KPS
Crystal Structure of the LC13 TCR in complex with HLA B*4405 bound to EEYLQAFTY a self peptide from the ABCD3 protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-01 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 142.518, 54.237, 121.766 |
| Unit cell angles | 90.00, 114.43, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.700 |
| R-factor | 0.197 |
| Rwork | 0.193 |
| R-free | 0.26900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 1SYV and 1KGC |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.202 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 5.810 | 2.700 |
| Rmerge | 0.071 | 0.030 | 0.295 |
| Number of reflections | 21530 | ||
| <I/σ(I)> | 11.7 | ||
| Completeness [%] | 92.0 | 100 | 55.6 |
| Redundancy | 3.3 | 3.6 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 277 | 0.2M NaOAc, 12-18% PEG 4000, 0.1M Tris, pH 8.5, vapor diffusion, hanging drop, temperature 277K |
