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 |