3MRG
Crystal Structure of MHC class I HLA-A2 molecule complexed with HCV NS3-1073-1081 nonapeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-12-02 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.93300 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.120, 80.870, 56.200 |
| Unit cell angles | 90.00, 112.33, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.300 |
| R-factor | 0.18 |
| Rwork | 0.179 |
| R-free | 0.20200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gso |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.231 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.5.0044) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.400 | |
| High resolution limit [Å] | 1.300 | 10.000 | 1.300 |
| Rmerge | 0.125 | 0.053 | 0.313 |
| Number of reflections | 104890 | 215 | 18701 |
| <I/σ(I)> | 10.15 | 20.4 | 2.8 |
| Completeness [%] | 97.2 | 82.7 | 87.3 |
| Redundancy | 4.53 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 17% PEG 6000, 0.1M NaCitrate, 0.05M NaCl, 5mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
