2FKL
Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain (Residues 126- 189 of APP)
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] | 295 |
Detector technology | AREA DETECTOR |
Collection date | 2003-07-26 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 44.694, 34.823, 50.810 |
Unit cell angles | 90.00, 98.53, 90.00 |
Refinement procedure
Resolution | 19.410 - 2.500 |
R-factor | 0.222 |
Rwork | 0.222 |
R-free | 0.26300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2fjz |
RMSD bond length | 0.007 |
RMSD bond angle | 1.200 |
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] | 20.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 5731 | |
<I/σ(I)> | 12.2 | 3.3 |
Completeness [%] | 81.8 | 52.4 |
Redundancy | 3.6 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.05 | 295 | 1.5 M (NH4)H2PO4, pH 4.05, VAPOR DIFFUSION, HANGING DROP, temperature 295K |