2FJZ
Structure of the Alzheimer's Amyloid Precursor Protein (APP) copper binding domain (residues 133 to 189) in 'small unit cell' form, metal-free
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 105 |
Detector technology | AREA DETECTOR |
Collection date | 2003-02-20 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 31.346, 32.518, 50.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 22.570 - 1.610 |
R-factor | 0.177 |
Rwork | 0.177 |
R-free | 0.20900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1owt |
RMSD bond length | 0.013 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.670 |
High resolution limit [Å] | 1.610 | 1.610 |
Number of reflections | 7043 | |
<I/σ(I)> | 15.5 | 5.4 |
Completeness [%] | 96.3 | 86.9 |
Redundancy | 2.7 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295 | 28 - 32 % (w/v) PEG 10000, 0.1 M HEPES pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |