1XR9
Crystal Structures of HLA-B*1501 in Complex with Peptides from Human UbcH6 and Epstein-Barr Virus EBNA-3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-07-20 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 0.84140 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.359, 81.389, 109.969 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.083 - 1.788 |
| R-factor | 0.17968 |
| Rwork | 0.177 |
| R-free | 0.23151 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | B*1501/LEKARGSTY Complex without Peptide |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.437 |
| Data scaling software | SCALA |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 31.654 | 1.870 |
| High resolution limit [Å] | 1.776 | 1.780 |
| Total number of observations | 19646 | |
| Number of reflections | 43204 | |
| <I/σ(I)> | 14.2 | 2.5 |
| Completeness [%] | 97.4 | 83.32 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 277 | 0.2M NH4Ac, 0.1M tri-Sodium Citrate dihydrate, pH 5.6, 30% w/v PEG4000, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
