3MRL
Crystal Structure of MHC class I HLA-A2 molecule complexed with HCV NS3-1073-1081 nonapeptide C6V variant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-11-11 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97569 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.634, 80.973, 57.019 |
| Unit cell angles | 90.00, 113.17, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.410 |
| R-factor | 0.205 |
| Rwork | 0.200 |
| R-free | 0.27900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3mrg |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.223 |
| 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] | 50.000 | 2.480 | |
| High resolution limit [Å] | 2.400 | 9.300 | 2.400 |
| Rmerge | 0.133 | 0.061 | 0.553 |
| Number of reflections | 16618 | 273 | 1495 |
| <I/σ(I)> | 7.82 | 12.2 | 2.9 |
| Completeness [%] | 93.9 | 84 | 90.2 |
| Redundancy | 2.99 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 15% PEG 6000, 0.1M NaCitrate, 3.6mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
