4JFN
Crystal structure of the N-terminal, growth factor-like domain of the amyloid precursor protein bound to copper
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-09-02 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.8726 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 34.050, 49.070, 66.160 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.276 - 1.750 |
R-factor | 0.1831 |
Rwork | 0.181 |
R-free | 0.23030 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mwp |
RMSD bond length | 0.007 |
RMSD bond angle | 1.156 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.280 | 1.810 |
High resolution limit [Å] | 1.750 | 1.750 |
Number of reflections | 11659 | |
Completeness [%] | 99.7 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 6% (w/v) PEG 3350, 0.1 M Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |