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 (%) |