9MDA
Conformational flexibility in HLA-B8: peptide tuning structural and dynamical changes
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2023-12-03 |
| Detector | MAR CCD 300 mm |
| Wavelength(s) | 0.87313 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.740, 81.550, 110.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.770 - 1.600 |
| R-factor | 0.20348 |
| Rwork | 0.202 |
| R-free | 0.23947 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6p2s |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.786 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.790 | 1.640 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.065 | |
| Number of reflections | 65307 | 3265 |
| <I/σ(I)> | 7.2 | |
| Completeness [%] | 100.0 | 78 |
| Redundancy | 6.4 | 3.5 |
| CC(1/2) | 0.998 | 0.862 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 12.5-16% PEG 4000,100mM citrate acid pH5.5 ,100mM ammonium acetate |
