1BX2
CRYSTAL STRUCTURE OF HLA-DR2 (DRA*0101,DRB1*1501) COMPLEXED WITH A PEPTIDE FROM HUMAN MYELIN BASIC PROTEIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE A1 |
| Synchrotron site | CHESS |
| Beamline | A1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-03-18 |
| Detector | ADSC |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 95.403, 95.403, 295.219 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.600 |
| R-factor | 0.238 |
| Rwork | 0.238 |
| R-free | 0.26600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dlh |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.500 |
| 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] | 20.000 | 2.600 |
| High resolution limit [Å] | 2.600 | 2.490 |
| Rmerge | 0.088 | 0.270 |
| Total number of observations | 263333 * | |
| Number of reflections | 42589 | |
| <I/σ(I)> | 23 | 3.9 |
| Completeness [%] | 88.3 | 83.1 |
| Redundancy | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 7.5 * | 18 * | 15-18% PEG6000 100MM GLYCINE PH3.5 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 10 (mg/ml) | |
| 2 | 1 | 1 | Tris-HCl | 50 (mM) | |
| 3 | 1 | 1 | glycine | 100 (mM) | |
| 4 | 1 | 1 | PEG6000 | 15-18 (%) |
