2FK1
Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'small unit cell' form, Cu(II)-bound
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-ID-B |
| Synchrotron site | APS |
| Beamline | 14-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-03-18 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.3784 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 31.437, 32.545, 50.402 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 16.830 - 1.600 |
| R-factor | 0.188 |
| Rwork | 0.188 |
| R-free | 0.23200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fjz |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.500 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Number of reflections | 7238 | |
| <I/σ(I)> | 22.1 | 5.7 |
| Completeness [%] | 95.5 | 66.5 |
| Redundancy | 5.6 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295 | 0.1 M HEPES pH 8.0, 28 - 32 % (w/v) PEG 10000, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
