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) |






