5U98
The crystal structure of a self-peptide complexed to Abacavir and HLA-B*57:01
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-08-30 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.9436 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.134, 132.602, 87.964 |
| Unit cell angles | 90.00, 104.99, 90.00 |
Refinement procedure
| Resolution | 28.323 - 2.000 |
| R-factor | 0.1739 |
| Rwork | 0.173 |
| R-free | 0.21650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3upr |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.052 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 28.323 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.270 |
| Number of reflections | 69488 |
| <I/σ(I)> | 30.398 |
| Completeness [%] | 95.0 |
| Redundancy | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 289 | 0.1M NACACODYLATE, 0.1MNAACETATE, 25% PEG 8,000, 15% GLYCEROL |
