5E61
Structure of amyloid-forming peptide FGAILSS (residues 23-29) 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 | 2014-04-25 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.979 |
Spacegroup name | P 1 |
Unit cell lengths | 8.770, 9.500, 24.740 |
Unit cell angles | 88.22, 80.00, 70.34 |
Refinement procedure
Resolution | 4.380 - 1.790 |
R-factor | 0.17221 |
Rwork | 0.167 |
R-free | 0.21833 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 2.000 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 4.380 | 1.960 |
High resolution limit [Å] | 1.790 | 1.790 |
Rmerge | 0.241 | 0.696 |
Number of reflections | 647 | |
<I/σ(I)> | 4.29 | 1.4 |
Completeness [%] | 93.4 | 72.3 |
Redundancy | 5.217 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 291 | 6.4mg/ml in 20mM Lithium hydroxide and mixed with 0.1M HEPES pH 6.5 and 0.5M Sodium Formate |