3MRK
Crystal Structure of MHC class I HLA-A2 molecule complexed with AFP137 nonapeptide
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 | 2006-09-01 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.07225 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.520, 79.890, 55.430 |
| Unit cell angles | 90.00, 111.85, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.400 |
| R-factor | 0.2 |
| Rwork | 0.200 |
| R-free | 0.23200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gso |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.247 |
| 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 | 1.500 | |
| High resolution limit [Å] | 1.400 | 10.000 | 1.400 |
| Rmerge | 0.055 | 0.037 | 0.383 |
| Number of reflections | 69080 | 44 | 13589 |
| <I/σ(I)> | 9.58 | 21.3 | 2.3 |
| Completeness [%] | 84.3 | 18.2 | 88.9 |
| Redundancy | 2.27 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 10% PEG 6000, 0.1M NaCitrate, 5mg/ml protein conc., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
