3MRD
Crystal Structure of MHC class I HLA-A2 molecule complexed with HCMV pp65-495-503 nonapeptide V6G variant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-06-18 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97949 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.140, 80.920, 56.200 |
| Unit cell angles | 90.00, 112.41, 90.00 |
Refinement procedure
| Resolution | 14.930 - 1.700 |
| R-factor | 0.196 |
| Rwork | 0.194 |
| R-free | 0.22600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gso |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.389 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.800 | |
| High resolution limit [Å] | 1.700 | 10.000 | 1.700 |
| Rmerge | 0.089 | 0.037 | 0.372 |
| Number of reflections | 47219 | 50 | 7487 |
| <I/σ(I)> | 12.42 | 18.2 | 5.5 |
| Completeness [%] | 97.4 | 19.2 | 98.7 |
| Redundancy | 3.99 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 10% PEG 6000, 0.1M MES, 5mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
