1M6O
Crystal Structure of HLA B*4402 in complex with HLA DPA*0201 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.805, 81.781, 110.069 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.600 |
| Rwork | 0.214 |
| R-free | 0.23400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1a1n |
| RMSD bond length | 0.005 |
| RMSD bond angle | 24.920 * |
| Data reduction software | d*TREK |
| Data scaling software | d*TREK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.049 | 0.276 |
| Total number of observations | 282153 * | |
| Number of reflections | 59302 | |
| <I/σ(I)> | 2 | |
| Completeness [%] | 96.8 | 92.7 * |
| Redundancy | 4.8 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 298 | Macdonald, W., (2002) FEBS Lett., 527, 27. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 3 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 20-30 (%) | pH5.2-5.9 |
| 3 | 1 | reservoir | citrate | 0.1 (M) | |
| 4 | 1 | reservoir | ammonium acetate | 0.2 (M) |
