1OR3
APOLIPOPROTEIN E3 (APOE3), TRIGONAL TRUNCATION MUTANT 165
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 125 |
Detector technology | AREA DETECTOR |
Collection date | 1997-05-15 |
Detector | ADSC |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 47.370, 47.370, 104.540 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 1.730 |
R-factor | 0.229 * |
Rwork | 0.229 |
R-free | 0.23800 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.100 |
Data reduction software | UCSD-system |
Data scaling software | UCSD-system |
Phasing software | SOLVE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.860 |
High resolution limit [Å] | 1.730 | 1.730 |
Rmerge | 0.068 | 0.225 |
Total number of observations | 48854 * | |
Number of reflections | 16782 | |
<I/σ(I)> | 27.4 | 3.7 |
Completeness [%] | 97.2 | 89.9 * |
Redundancy | 2.9 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.6 | RT, 50MM NA-CACODYLATE, PH 5.6, 10-20% PEG 400, 1% 2-ME. NOTE: W/O 2-ME OR HIGHER PEG CONCENTRATIONS, OTHER CRYSTAL FORMS APPEARS (SEE PDB ENTRIES 1BZ4, 1OR2). |
Crystallization Reagents
ID | crystal ID | solution ID | reagent name | concentration | details |
1 | 1 | 2 | 50MM NA-Cacodylate, pH 5.6 | ||
2 | 1 | 2 | 10-20% PEG 400 | ||
3 | 1 | 2 | 1% 2-ME |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG400 | 20-25 (%) | |
2 | 1 | reservoir | sodium cacodylate | 50 (mM) | |
3 | 1 | drop | 20 (mM) | ||
4 | 1 | drop | protein | 5 (mg/ml) |