3MRM
Crystal Structure of MHC class I HLA-A2 molecule complexed with HCV NS3-1406-1415 decapeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-10-30 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.979743 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.223, 80.985, 56.341 |
| Unit cell angles | 90.00, 112.24, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.900 |
| R-factor | 0.192 |
| Rwork | 0.190 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gso |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.143 |
| 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] | 25.000 | 1.970 | |
| High resolution limit [Å] | 1.900 | 7.360 | 1.900 |
| Rmerge | 0.102 | 0.056 | 0.330 |
| Number of reflections | 32805 | 607 | 3039 |
| <I/σ(I)> | 11.16 | 26.6 | 2.9 |
| Completeness [%] | 93.8 | 95.3 | 85.1 |
| Redundancy | 4.11 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 18% PEG 6000, 0.1M NaCitrate, 0.02M NaCl, 5mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
