8ANH
Structure of the amyloid-forming peptide LYIQWL from Tc5b, grown from 30% acetonitrile
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU PhotonJet-R |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-09-07 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.54184 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 11.744, 23.164, 18.715 |
| Unit cell angles | 90.00, 90.23, 90.00 |
Refinement procedure
| Resolution | 14.560 - 1.250 |
| R-factor | 0.1017 |
| Rwork | 0.098 |
| R-free | 0.13740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | ideal 5 residue beta strand form the software Fragon |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.084 |
| 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] | 14.560 | 1.290 |
| High resolution limit [Å] | 1.250 | 1.250 |
| Rmeas | 0.139 | 0.468 |
| Number of reflections | 2829 | 284 |
| <I/σ(I)> | 9.2 | 3.1 |
| Completeness [%] | 99.3 | 97.26 |
| Redundancy | 6.6 | |
| CC(1/2) | 0.998 | 0.777 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION, RECRYSTALLIZATION | 310 | Peptide was dissolved in 30% acetonitrile at 0.2 mg/ml concentration and incubated at 310K |
