3MRP
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 | 2007-05-04 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9500 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.473, 80.952, 56.961 |
| Unit cell angles | 90.00, 113.15, 90.00 |
Refinement procedure
| Resolution | 14.660 - 2.100 |
| R-factor | 0.187 |
| Rwork | 0.184 |
| R-free | 0.22700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3mrg |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.140 |
| 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 | 2.170 | |
| High resolution limit [Å] | 2.100 | 8.130 | 2.100 |
| Rmerge | 0.068 | 0.031 | 0.236 |
| Number of reflections | 25947 | 465 | 2280 |
| <I/σ(I)> | 13.68 | 27.7 | 4.7 |
| Completeness [%] | 99.1 | 97.3 | 94.1 |
| Redundancy | 3.65 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 13% PEG 6000, 0.1M NaCitrate, 0.1M NaCl, 2.61mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
