8ANK
Structure of the amyloid-forming peptide pEFIAWL 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 | 2021-07-29 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.54184 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 20.710, 9.545, 22.396 |
| Unit cell angles | 90.00, 92.74, 90.00 |
Refinement procedure
| Resolution | 11.190 - 1.300 |
| R-factor | 0.1039 |
| Rwork | 0.101 |
| R-free | 0.12980 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | ideal 5 residue beta strand form the software Fragon |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.911 |
| Data reduction software | CrysalisPro |
| Data scaling software | CrysalisPro |
| Phasing software | Fragon |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 11.190 | 1.350 |
| High resolution limit [Å] | 1.300 | 1.300 |
| Rmeas | 0.106 | 0.331 |
| Number of reflections | 1157 | 114 |
| <I/σ(I)> | 13.6 | 3.9 |
| Completeness [%] | 99.8 | 99.13 |
| Redundancy | 4.78 | |
| CC(1/2) | 0.995 | 0.893 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION, RECRYSTALLIZATION | 310 | EFIAWL was dissolved in 0.15 - 0.5 mg/ml concentration in a solution containing 30 % acetonitrile and 0.1 % TFA and incubated at 310K for several weeks. |
