1UXS
CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE LATENT MEMBRANE PROTEIN 2 PEPTIDE (LMP2)OF EPSTEIN-BARR VIRUS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-06-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.136, 82.329, 65.910 |
| Unit cell angles | 90.00, 109.25, 90.00 |
Refinement procedure
| Resolution | 62.020 - 1.550 |
| R-factor | 0.143 |
| Rwork | 0.142 |
| R-free | 0.17700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1k5n |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.470 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.19) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 62.000 | 1.610 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.051 | 0.246 |
| Number of reflections | 74438 | |
| <I/σ(I)> | 21 | 4 |
| Completeness [%] | 99.0 | 97 |
| Redundancy | 3.3 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 0.1M TRIS, PH 7.5, 15% PEG8000 |
