1JHT
Crystal structure of HLA-A2*0201 in complex with a nonameric altered peptide ligand (ALGIGILTV) from the MART-1/Melan-A.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-03-26 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.190, 74.470, 122.290 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.690 - 2.150 |
| R-factor | 0.21 |
| Rwork | 0.210 |
| R-free | 0.25200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1DUZ (peptide removed) |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.250 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.039 | 0.124 |
| Total number of observations | 190647 * | |
| Number of reflections | 25511 | 3085 * |
| <I/σ(I)> | 36 | 8.2 |
| Completeness [%] | 99.0 | 96.4 |
| Redundancy | 7.4 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 20 * | 16% PEG, 25 mM MES, 0.10% NaN3, pH 6.5, VAPOR DIFFUSION, HANGING DROP, at 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | MES | 25 (mM) | |
| 3 | 1 | reservoir | PEG6000 | 16 (%) | |
| 4 | 1 | reservoir | MES | 25 (mM) | |
| 5 | 1 | reservoir | 0.10 (%) |
