5E5X
Structure of the amyloid forming peptide ANFLVH (residues 13-18) from islet amyloid polypeptide
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 | 2009-11-24 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.979 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 4.831, 39.726, 9.869 |
Unit cell angles | 90.00, 103.69, 90.00 |
Refinement procedure
Resolution | 19.863 - 1.610 |
R-factor | 0.1179 |
Rwork | 0.113 |
R-free | 0.16120 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.003 |
RMSD bond angle | 0.704 |
Data reduction software | DENZO |
Phasing software | PHASER |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 90.000 | 1.720 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.147 | |
Number of reflections | 433 | |
<I/σ(I)> | 6.55 | 9.7 |
Completeness [%] | 93.3 | 87 |
Redundancy | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | 20 mg/ml in water and mixed with 10% (w/v) PEG-8000, 0.1 M Na/K phosphate pH 6.2, and 0.2 M NaCl |