2FMA
Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'small unit cell' form, atomic resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 14-BM-C |
Synchrotron site | APS |
Beamline | 14-BM-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-07-20 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 31.289, 32.488, 50.088 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 13.850 - 0.850 |
R-factor | 0.1305 |
Rwork | 0.131 |
R-free | 0.14970 |
Structure solution method | Rigid body refinement |
Starting model (for MR) | 2fjz |
RMSD bond length | 0.026 |
RMSD bond angle | 0.036 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELX |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 0.870 |
High resolution limit [Å] | 0.850 | 0.850 |
Number of reflections | 41418 | |
<I/σ(I)> | 1.7 | |
Completeness [%] | 90.5 | 43.8 |
Redundancy | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295 | 0.1M HEPES pH 8.0, 28-32% (w/v) PEG 10000, VAPOR DIFFUSION, HANGING DROP, temperature 295K |