1LE2
STRUCTURAL BASIS FOR ALTERED FUNCTION IN THE COMMON MUTANTS OF HUMAN APOLIPOPROTEIN-E
Experimental procedure
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 41.060, 53.940, 83.910 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 * - 3.000 |
| Rwork | 0.195 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 3.700 |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 10.000 * |
| High resolution limit [Å] | 3.000 * |
| Number of reflections | 2749 * |
| Completeness [%] | 67.9 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5.3 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | ||
| 2 | 1 | reservior | PEG400 | 15 (%) | |
| 3 | 1 | reservoir | sodium acetate | 20 (mM) | |
| 4 | 1 | reservoir | beta-n-octylglucopyranoide | 0.2 (%) | |
| 5 | 1 | reservoir | beta-mercaptoethanol | 0.1 (%) |
