5E5Z
Structure of the amyloid forming peptide LVHSSN (residues
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 291 |
Detector technology | CCD |
Collection date | 2010-03-10 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.979 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 9.643, 9.609, 19.029 |
Unit cell angles | 90.00, 101.22, 90.00 |
Refinement procedure
Resolution | 9.459 - 1.664 |
R-factor | 0.1702 |
Rwork | 0.167 |
R-free | 0.19830 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.975 |
Data reduction software | DENZO |
Phasing software | PHASER |
Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 100.000 |
High resolution limit [Å] | 1.600 |
Rmerge | 0.076 |
Number of reflections | 1136 |
<I/σ(I)> | 17.86 |
Completeness [%] | 92.9 |
Redundancy | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | 20 mg/ml in water and mixed with 0.09 M HEPES pH 7.5, 1.26M tri-sodium citrate, and 10% glycerol |