29VU
Structure of the amyloid-forming peptide Ac-LLQDIM-NH2 from human GHRH
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU PhotonJet-R |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-02-29 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.54184 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 38.760, 4.830, 24.400 |
| Unit cell angles | 90.00, 112.01, 90.00 |
Refinement procedure
| Resolution | 17.970 - 1.410 |
| R-factor | 0.1393 |
| Rwork | 0.137 |
| R-free | 0.17240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.368 |
| Data reduction software | autoPROC |
| Data scaling software | XSCALE |
| Phasing software | Fragon |
| Refinement software | PHENIX (1.21.2_5419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 17.970 | 1.518 |
| High resolution limit [Å] | 1.379 | 1.379 |
| Rmeas | 0.105 | 0.825 |
| Number of reflections | 945 | 164 |
| <I/σ(I)> | 6.5 | |
| Completeness [%] | 92.5 | |
| Redundancy | 3.5 | |
| CC(1/2) | 0.996 | 0.398 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION, RECRYSTALLIZATION | 310 | crystals formed on the wall of the tube during overnight incubation at 310 K from a 5 mg / ml solution at pH 4 |
