8YG2
Crystal structure of amyloidogenic peptide Piv-NFGAIL-NH2 from Islet Amyloid Polypeptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-1A |
Synchrotron site | Photon Factory |
Beamline | BL-1A |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-10-21 |
Detector | DECTRIS EIGER X 4M |
Wavelength(s) | 1.040 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 4.864, 20.466, 20.855 |
Unit cell angles | 90.00, 88.60, 90.00 |
Refinement procedure
Resolution | 20.470 - 1.250 |
Rwork | 0.174 |
R-free | 0.20100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.733 |
Data reduction software | DIALS (2.2.10) |
Data scaling software | DIALS (2.2.10) |
Phasing software | PHASER (2.8.3) |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.470 | 1.270 |
High resolution limit [Å] | 1.250 | 1.250 |
Rmerge | 0.084 | 0.155 |
Number of reflections | 1063 | 55 |
<I/σ(I)> | 59.11 | |
Completeness [%] | 91.9 | 94.8 |
Redundancy | 2 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 298 | Formic acid |