9NKH
Conformational flexibility in HLA-B8: peptide tuning structural and dynamical changes
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX IV BEAMLINE BioMAX |
| Synchrotron site | MAX IV |
| Beamline | BioMAX |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2024-11-15 |
| Detector | AGILENT ATLAS CCD |
| Wavelength(s) | 0.72932 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 68.684, 86.013, 70.432 |
| Unit cell angles | 90.00, 99.59, 90.00 |
Refinement procedure
| Resolution | 27.020 - 1.940 |
| R-factor | 0.2389 |
| Rwork | 0.238 |
| R-free | 0.25900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.796 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.21.1_5286)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 69.450 | 1.969 |
| High resolution limit [Å] | 1.936 | 1.936 |
| Rmerge | 0.115 | |
| Number of reflections | 56956 | 2682 |
| <I/σ(I)> | 5.3 | 1.2 |
| Completeness [%] | 94.5 | 88.6 |
| Redundancy | 6.7 | |
| CC(1/2) | 0.330 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.4 | 298 | 25% PEG3350, 0.1M Tris pH8.4, 0.1M (NH4)2SO4, 90mM Cesium chloride |
