3BVN
High resolution crystal structure of HLA-B*1402 in complex 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 | CCD |
| Collection date | 2007-04-17 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.91841 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.383, 79.953, 105.440 |
| Unit cell angles | 90.00, 99.51, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.550 |
| R-factor | 0.2402 |
| Rwork | 0.240 |
| R-free | 0.26840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1uxw |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.630 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.640 |
| High resolution limit [Å] | 2.550 | 2.550 |
| Rmerge | 0.137 | |
| Number of reflections | 26731 | |
| <I/σ(I)> | 8.87 | |
| Completeness [%] | 93.2 | 76.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 20-22%(w/v) PEG 20 000, 0.1 M HEPES buffer pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
