1H15
X-ray crystal structure of HLA-DRA1*0101/DRB5*0101 complexed with a peptide from Epstein Barr Virus DNA polymerase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 293 |
| Detector technology | CCD |
| Collection date | 2001-02-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 65 |
| Unit cell lengths | 179.244, 179.244, 92.884 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.880 - 3.100 |
| R-factor | 0.256 |
| Rwork | 0.256 |
| R-free | 0.31000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | SINGLE COPY OF 1FV1 (A AND B CHAINS) MINUS PEPTIDE |
| RMSD bond length | 0.008 |
| RMSD bond angle | 26.100 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.300 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Rmerge | 0.414 | 0.774 |
| Total number of observations | 166287 * | |
| Number of reflections | 28750 | |
| <I/σ(I)> | 5.7 | 1.1 |
| Completeness [%] | 94.5 | 78.9 |
| Redundancy | 6 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.4 * | 18 * | 14% PEG 3550, 100MM GLYCINE AND 10MM TRIS AT PH 3.5-4.0. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Tris | 10 (mM) | pH7.4 |
| 2 | 1 | drop | protein | 10 (mg/ml) | |
| 3 | 1 | reservoir | PEG3350 | 14 (%) | |
| 4 | 1 | reservoir | glycine | 100 (mM) | |
| 5 | 1 | reservoir | Tris | 10 (mM) | pH3.5-4.0 |
