1E28
Nonstandard peptide binding of HLA-B*5101 complexed with HIV immunodominant epitope KM2(TAFTIPSI)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.900, 83.000, 111.800 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 - 3.000 |
| R-factor | 0.194 |
| Rwork | 0.194 |
| R-free | 0.25300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | HLA B53 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 24.900 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 3.110 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.120 | 0.249 |
| Total number of observations | 38887 * | |
| Number of reflections | 8737 * | |
| <I/σ(I)> | 11.8 | 3.9 |
| Completeness [%] | 83.0 | 64.5 |
| Redundancy | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8 * | 21 * | pH 6.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris | 20 (mM) | |
| 3 | 1 | reservoir | PEG4000 | 20 (%) | |
| 4 | 1 | reservoir | HEPES | 0.1 (M) | |
| 5 | 1 | reservoir | isopropanol | 10 (%) |
