1NFO
APOLIPOPROTEIN E2 (APOE2, D154A MUTATION)
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 130 |
| Detector technology | AREA DETECTOR |
| Detector | ADSC |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.613, 53.671, 84.795 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.000 |
| R-factor | 0.206 |
| R-free | 0.27000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PHASING MODEL DERIVED FROM 1NFN |
| RMSD bond length | 0.010 |
| RMSD bond angle | 2.000 |
| Phasing software | SHELXL-93 |
| Refinement software | SHELXL-93 |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 15.000 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.051 |
| Number of reflections | 8964 * |
| Completeness [%] | 94.2 |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | Wilson, C., (1991) Science, 252, 1817. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | PEG400 | 15 (%) | |
| 3 | 1 | drop | sodium acetate | 20 (mM) | |
| 4 | 1 | drop | beta-n-octylglucopyranoside | 0.2 (%) | |
| 5 | 1 | drop | beta-mercaptoethanol | 0.1 (%) |
