3QDJ
The complex between TCR DMF5 and human Class I MHC HLA-A2 with the bound MART-1(27-35) nonameric peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-25 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.98 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 227.774, 46.305, 85.859 |
| Unit cell angles | 90.00, 106.55, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-factor | 0.2435 |
| Rwork | 0.240 |
| R-free | 0.29910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2gj6 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.562 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 20.000 | 20.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 6.180 | 2.300 |
| Rmerge | 0.071 | 0.048 | 0.410 |
| Number of reflections | 37500 | ||
| <I/σ(I)> | 19.1 | ||
| Completeness [%] | 97.0 | 94.6 | 81.5 |
| Redundancy | 3.6 | 3.3 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 297 | PEG 24%, TRIS 0.1M, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K |
