3MRF
Crystal Structure of MHC class I HLA-A2 molecule complexed with EBV bmlf1-280-288 nonapeptide T4P 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 | 2006-07-21 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.93300 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.622, 79.392, 55.661 |
| Unit cell angles | 90.00, 112.02, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.300 |
| R-factor | 0.189 |
| Rwork | 0.186 |
| R-free | 0.25700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3mre |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.142 |
| 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 | 2.380 | |
| High resolution limit [Å] | 2.300 | 8.910 | 2.300 |
| Rmerge | 0.110 | 0.029 | 0.401 |
| Number of reflections | 18522 | 315 | 1763 |
| <I/σ(I)> | 11.8 | 32.5 | 3.6 |
| Completeness [%] | 99.3 | 92.9 | 97.6 |
| Redundancy | 3.74 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 12% PEG 6000, 0.1M NaCacodylate, 0.1M NaCl, 7.5mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
