2AV1
Crystal structure of HTLV-1 TAX peptide Bound to Human Class I MHC HLA-A2 with the E63Q and K66A mutations 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 | 2004-04-17 |
| Detector | CUSTOM-MADE |
| Wavelength(s) | 0.97951 |
| Spacegroup name | P 1 |
| Unit cell lengths | 50.328, 62.536, 74.747 |
| Unit cell angles | 82.10, 76.39, 78.10 |
Refinement procedure
| Resolution | 10.000 - 1.950 |
| R-factor | 0.17724 |
| Rwork | 0.174 |
| R-free | 0.23059 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1duz |
| RMSD bond length | 0.021 |
| RMSD bond angle | 2.048 |
| 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 | 2.020 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.072 | 0.302 |
| Number of reflections | 61476 | |
| <I/σ(I)> | 10.29 | 2.22 |
| Completeness [%] | 96.4 | 91.2 |
| Redundancy | 1.9 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | PEG3350 20%, MES 0.025M, NaSCN 0.1M, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
