8QWU
Structure of the amyloid-forming peptide LYIQNL, grown without ethanol
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU PhotonJet-R |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-06-20 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.54184 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 4.848, 20.005, 42.650 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.110 - 1.550 |
| R-factor | 0.2352 |
| Rwork | 0.234 |
| R-free | 0.24370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.034 |
| 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] | 18.110 | 1.610 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmeas | 0.160 | 0.414 |
| Number of reflections | 706 | 53 |
| <I/σ(I)> | 7.4 | 3.5 |
| Completeness [%] | 94.0 | 68.83 |
| Redundancy | 4.83 | |
| CC(1/2) | 0.998 | 0.920 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION, RECRYSTALLIZATION | 4.8 | 310 | the peptide was dissolved in 0.1M acetate buffer, pH 4.80 at 0.12 mg/mL concentration and incubated at 310K |
