3MRO
Crystal Structure of MHC class I HLA-A2 molecule complexed with Melan-A MART1 decapeptide variant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-05-25 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.072 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.881, 81.076, 57.276 |
| Unit cell angles | 90.00, 113.80, 90.00 |
Refinement procedure
| Resolution | 14.470 - 2.350 |
| R-factor | 0.224 |
| Rwork | 0.219 |
| R-free | 0.27900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3mrp |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.265 |
| 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] | 50.000 | 2.430 | |
| High resolution limit [Å] | 2.350 | 9.100 | 2.350 |
| Rmerge | 0.110 | 0.052 | 0.315 |
| Number of reflections | 18709 | 307 | 1752 |
| <I/σ(I)> | 8.95 | 16.9 | 3.8 |
| Completeness [%] | 98.8 | 89.8 | 97.3 |
| Redundancy | 3.53 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 12% PEG 6000, 0.1M NaCitrate, 0.1M NaCl, 3mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
