3MRB
Crystal Structure of MHC class I HLA-A2 molecule complexed with HCMV pp65-495-503 nonapeptide A7H variant
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 | 2006-07-03 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.93300 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.360, 81.090, 56.790 |
| Unit cell angles | 90.00, 112.93, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.400 |
| R-factor | 0.214 |
| Rwork | 0.212 |
| R-free | 0.24400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gso |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.295 |
| 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 | 1.450 | |
| High resolution limit [Å] | 1.400 | 5.420 | 1.400 |
| Rmerge | 0.066 | 0.033 | 0.320 |
| Number of reflections | 84555 | 1424 | 8317 |
| <I/σ(I)> | 13.07 | 33.1 | 3.2 |
| Completeness [%] | 96.5 | 90.6 | 95.1 |
| Redundancy | 4.21 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 12% PEG 6000, 0.1M NaCacodylate, 5mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
