2FK3
Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'large unit cell' form
Experimental procedure
| Experimental method | MAD |
| 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 | 2003-11-13 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.3786 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 59.623, 67.437, 127.656 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.880 - 2.400 |
| R-factor | 0.208 |
| Rwork | 0.208 |
| R-free | 0.24800 |
| Structure solution method | SAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.900 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Number of reflections | 20981 | |
| <I/σ(I)> | 30.8 | 9.3 |
| Completeness [%] | 98.5 | 86.3 |
| Redundancy | 11.4 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.4 | 295 | 0.1 M MES pH 5.4 - 5.6, 0.4 M NaCOOH, 10 - 15 % (w/v) PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
