1GS9
Apolipoprotein E4, 22k domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 125 |
Detector technology | CCD |
Collection date | 1999-04-15 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.511, 53.089, 73.372 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.900 - 1.700 |
R-factor | 0.219 |
Rwork | 0.218 |
R-free | 0.24700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bz4 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.794 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | EPMR |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.900 |
High resolution limit [Å] | 1.700 |
Number of reflections | 20168 |
<I/σ(I)> | 12.1 |
Completeness [%] | 100.0 |
Redundancy | 7.7 |
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, CRYSTALLIZED FROM FULL LENGTH APOE4 CONSTRUCT (299 RESIDUES). PROTEOLYTIC CLEAVAGE IN CRYSTALLIZATION DROP TO 22K FRAGMENT. NEW, THIRD ORTHOGONAL CRYSTAL FORM OF APOE (ORTHO-3) |