5WMP
Crystal Structure of HLA-B7 in complex with TPR, a CMV peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-12-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.954 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.863, 81.720, 110.943 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.240 - 1.600 |
| R-factor | 0.1739 |
| Rwork | 0.172 |
| R-free | 0.19870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.000 |
| Data scaling software | Aimless (0.1.2) |
| Phasing software | PHASER |
| Refinement software | BUSTER |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 46.240 | 46.240 | 1.630 |
| High resolution limit [Å] | 1.600 | 8.640 | 1.600 |
| Rmerge | 0.127 | 0.067 | 0.866 |
| Rmeas | 0.137 | 0.073 | 0.933 |
| Rpim | 0.050 | 0.030 | 0.344 |
| Total number of observations | 444657 | 2642 | 21277 |
| Number of reflections | 61273 | 450 | 2971 |
| <I/σ(I)> | 10.3 | 25.7 | 2 |
| Completeness [%] | 99.9 | 97.3 | 97.9 |
| Redundancy | 7.3 | 5.9 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | 18-24%PEG4000, 0.2 NH4 Acetate, 0.1M Na-cacodylate pH 6.5 |
