1B68
APOLIPOPROTEIN E4 (APOE4), 22K FRAGMENT
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 125 |
| Detector technology | CCD |
| Collection date | 1998-03 |
| Detector | ADSC |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.210, 53.210, 84.760 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.000 |
| R-factor | 0.2 |
| Rwork | 0.200 |
| R-free | 0.25500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bz4 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 19.800 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.980 |
| High resolution limit [Å] | 1.840 | 1.840 |
| Rmerge | 0.037 | 0.199 |
| Number of reflections | 16493 | |
| <I/σ(I)> | 27.4 | 3.7 |
| Completeness [%] | 99.1 | 98.7 |
| Redundancy | 4.9 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.2 * | 298 | WELL : 28% PEG 400, 20MM NAOAC, PH 6.0, 0.1% BME PROTEIN SOLN: 40MM (NH4)H(CO3), 7MG/ML PROTEIN DROPS : WELL/PROTEIN 1/3, ROOM TEMPERATURE, pH 6.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG400 | 22 (%) | |
| 2 | 1 | reservoir | sodium acetate | 20 (mM) | |
| 3 | 1 | reservoir | beta-mercaptoethanol | 0.1 (%) |






