1AKJ
COMPLEX OF THE HUMAN MHC CLASS I GLYCOPROTEIN HLA-A2 AND THE T CELL CORECEPTOR CD8
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-02-13 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 70.900, 89.600, 116.000 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 2.650 |
| R-factor | 0.206 |
| Rwork | 0.206 |
| R-free | 0.27600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 3HLA 1cd8 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 26.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.710 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Rmerge | 0.095 * | 0.446 * |
| Total number of observations | 77731 * | |
| Number of reflections | 21379 | |
| <I/σ(I)> | 15.2 | 2.6 |
| Completeness [%] | 96.5 | 96.4 |
| Redundancy | 3.7 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 6.5 | PROTEIN WAS CRYSTALLIZED FROM 12% PEG 20000, 100 MM MES, PH 6.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 10 (mM) | ||
| 4 | 1 | drop | CD8alphaalpha | 10 (mg/ml) | |
| 5 | 1 | reservoir | PEG20000 | 12 (%) | |
| 6 | 1 | reservoir | MES | 100 (mM) |
