2AV7
Crystal structure of HTLV-1 TAX peptide Bound to Human Class I MHC HLA-A2 with the K66A mutation in the heavy chain.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-08-21 |
| Detector | CUSTOM-MADE |
| Wavelength(s) | 0.97925 |
| Spacegroup name | P 1 |
| Unit cell lengths | 50.320, 62.532, 74.801 |
| Unit cell angles | 82.13, 76.57, 78.06 |
Refinement procedure
| Resolution | 10.000 - 2.050 |
| R-factor | 0.17472 |
| Rwork | 0.171 |
| R-free | 0.23408 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1duz |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.943 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.120 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.075 | 0.280 |
| Number of reflections | 53990 | |
| <I/σ(I)> | 10.5 | 2.34 |
| Completeness [%] | 95.5 | 83.7 |
| Redundancy | 1.9 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | PEG3350 24%, MES 0.025M., pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
