7N6D
HLA peptide complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-10-09 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.953731 |
| Spacegroup name | P 31 1 2 |
| Unit cell lengths | 85.197, 85.197, 442.850 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.280 - 2.300 |
| R-factor | 0.2144 |
| Rwork | 0.213 |
| R-free | 0.24700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gso |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.654 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.210 | 2.340 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.165 | 1.782 |
| Rmeas | 0.160 | |
| Rpim | 0.060 | 0.482 |
| Number of reflections | 82685 | 4473 |
| <I/σ(I)> | 10.3 | 1.5 |
| Completeness [%] | 99.9 | 99.95 |
| Redundancy | 14 | 14.4 |
| CC(1/2) | 0.997 | 0.997 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293.15 | 20% PEG3350, 0.2 M sodium thiocyanate |
