1AOX
I DOMAIN FROM INTEGRIN ALPHA2-BETA1
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 287 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-11 |
| Detector | RIGAKU |
| Spacegroup name | P 1 |
| Unit cell lengths | 40.540, 43.290, 68.040 |
| Unit cell angles | 88.27, 76.59, 66.74 |
Refinement procedure
| Resolution | 15.000 - 2.100 |
| R-factor | 0.219 |
| Rwork | 0.219 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ido |
| RMSD bond length | 0.020 |
| RMSD bond angle | 26.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.8) |
| Refinement software | X-PLOR (3.8) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.230 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Number of reflections | 23946 | |
| <I/σ(I)> | 21.8 | 9.7 |
| Completeness [%] | 99.5 | 99.5 |
| Redundancy | 3.2 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | Emsley, J., (1997) J. Biol. Chem., 272, 28512. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | PEG8000 | 16-20 (%) | |
| 3 | 1 | reservoir | HEPES | 50 (mM) | |
| 4 | 1 | reservoir | 10 (mM) | ||
| 5 | 1 | reservoir | glycerol | 20 (%) |






