31VO
Crystal structure of amyloid beta 1-15 fragment bound to HLA-DR1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALBA BEAMLINE XAIRA |
| Synchrotron site | ALBA |
| Beamline | XAIRA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2026-06-16 |
| Detector | DECTRIS EIGER2 XE 9M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 57.308, 118.508, 67.126 |
| Unit cell angles | 90.00, 109.15, 90.00 |
Refinement procedure
| Resolution | 31.710 - 2.000 |
| R-factor | 0.1906 |
| Rwork | 0.189 |
| R-free | 0.22020 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.835 |
| Data reduction software | xia2 |
| Data scaling software | Aimless |
| Phasing software | PHASER (2.8.3) |
| Refinement software | PHENIX (2.0_5936) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.910 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.153 | 1.580 |
| Rmeas | 0.165 | 1.750 |
| Rpim | 0.063 | 0.737 |
| Number of reflections | 56684 | 4148 |
| <I/σ(I)> | 7.7 | 1.9 |
| Completeness [%] | 99.3 | 98.2 |
| Redundancy | 6.8 | 5.7 |
| CC(1/2) | 0.993 | 0.395 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2 M MgCl2, 0.1 M TRIS pH 8.5, 25% PEG 3350 |
