3D18
Crystal structure of HLA-B*2709 complexed with a variant of the latent membrane protein 2 peptide (LMP2(L)) 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 | CCD |
| Collection date | 2006-08-30 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.91841 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.753, 82.560, 108.993 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 24.020 - 1.740 |
| R-factor | 0.19404 |
| Rwork | 0.192 |
| R-free | 0.23251 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1uxs |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.189 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.800 |
| High resolution limit [Å] | 1.740 | 1.740 |
| Rmerge | 0.069 | 0.396 |
| Number of reflections | 46874 | |
| <I/σ(I)> | 7.5 | |
| Completeness [%] | 98.1 | 85.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 291 | 20% PEG 4000, 0.1M MES, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
