8ONQ
Structure of the amyloid-forming peptide Ac-EFIAWL from human GLP-1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU PhotonJet-R |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-01-11 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.54184 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 9.536, 42.631, 11.197 |
| Unit cell angles | 90.00, 95.68, 90.00 |
Refinement procedure
| Resolution | 10.780 - 1.500 |
| R-factor | 0.1536 |
| Rwork | 0.151 |
| R-free | 0.17370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.941 |
| Data reduction software | CrysalisPro |
| Data scaling software | CrysalisPro |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.780 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmeas | 0.135 | 0.632 |
| Number of reflections | 1419 | 153 |
| <I/σ(I)> | 6.2 | 1.2 |
| Completeness [%] | 97.5 | 93.29 |
| Redundancy | 3 | |
| CC(1/2) | 0.995 | 0.699 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION, RECRYSTALLIZATION | 310 | Ac-EFIAWL was dissolved in 0.016 mg/ml concentration in 0.1M citrate, pH 4.0 and incubated at 310K. |
