29VT
Structure of the amyloid-forming peptide Ac-YLESLM-OH from human PHM
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU PhotonJet-R |
| Temperature [K] | 310 |
| Detector technology | PIXEL |
| Collection date | 2024-06-24 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.54184 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 27.290, 9.510, 19.010 |
| Unit cell angles | 90.00, 118.57, 90.00 |
Refinement procedure
| Resolution | 13.160 - 1.250 |
| R-factor | 0.0915 |
| Rwork | 0.091 |
| R-free | 0.09600 |
| Structure solution method | AB INITIO PHASING |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.201 |
| Data reduction software | autoPROC |
| Data scaling software | XSCALE |
| Phasing software | SHELXT |
| Refinement software | PHENIX (1.21.2_5419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 13.164 | 1.371 |
| High resolution limit [Å] | 1.246 | 1.246 |
| Rmeas | 0.073 | 0.316 |
| Number of reflections | 1210 | 243 |
| <I/σ(I)> | 14.4 | 3.1 |
| Completeness [%] | 94.1 | |
| Redundancy | 3.4 | |
| CC(1/2) | 0.998 | 0.837 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION, RECRYSTALLIZATION | 310 | the peptide was dissolved at 1 mg/ml in water containing 30% (v/v) acetonitrile (pH 4) and incubated at 310 K |
