1H7I
Apolipoprotein E3 22kD fragment LYS146GLN mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 120 |
Collection date | 1995-03-15 |
Detector | ADSC ADSC MULTIWIRE |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.700, 52.960, 84.420 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.900 |
R-factor | 0.205 |
Rwork | 0.203 |
R-free | 0.25900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bz4 |
RMSD bond length | 0.037 |
Data reduction software | ADSC |
Data scaling software | ADSC |
Phasing software | EPMR |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.950 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.041 | 0.247 |
Number of reflections | 14706 | |
<I/σ(I)> | 22.4 | 2 |
Completeness [%] | 98.0 | 96.6 |
Redundancy | 3.3 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.6 | 50MM NA-CACODYLATE, PH 5.6, 20-25% PEG 400, 1% 2-ME. RT. ORTHORHOMBIC FORM ORTHO-2 APPEARS (SEE PDB ENTRY 1OR2). |