29VS
Structure of the amyloid-forming peptide YLESLM from human PHM
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU PhotonJet-R |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-01-24 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.54184 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 4.833, 18.483, 43.363 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 21.680 - 1.050 |
| R-factor | 0.1909 |
| Rwork | 0.189 |
| R-free | 0.21040 |
| Structure solution method | AB INITIO PHASING |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.528 |
| Data reduction software | CrysalisPro |
| Data scaling software | CrysalisPro |
| Phasing software | SHELXT |
| Refinement software | PHENIX (1.21.2_5419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 21.690 | 1.090 |
| High resolution limit [Å] | 1.050 | 1.050 |
| Rmeas | 0.219 | 1.351 |
| Number of reflections | 2136 | 201 |
| <I/σ(I)> | 5.4 | 1.8 |
| Completeness [%] | 100.0 | |
| Redundancy | 4.49 | |
| CC(1/2) | 0.994 | 0.605 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION, RECRYSTALLIZATION | 310 | the peptide was dissolved in 0.2 M acetate buffer (pH 4.67) at a concentration of 5 mg/ml and incubated at 310 K |
