1LE4
STRUCTURAL BASIS FOR ALTERED FUNCTION IN THE COMMON MUTANTS OF HUMAN APOLIPOPROTEIN-E
Experimental procedure
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.710, 53.330, 85.280 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | ? - 2.500 |
Rwork | 0.175 |
RMSD bond length | 0.015 |
RMSD bond angle | 3.100 |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.500 * |
Number of reflections | 6752 * |
Completeness [%] | 99.1 * |
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 | 10 (mg/ml) | |
2 | 1 | reservior | sodium acetate | 20 (mM) | |
3 | 1 | reservoir | beta-n-glycopyranoside | 0.2 (%) | |
4 | 1 | reservoir | PEG400 | 15 (%) |