9EK4
Crystal structure of HLA-B*07:02 with the 9-mer TP53 mutant peptide MPILTIITL
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS-II BEAMLINE 19-ID |
| Synchrotron site | NSLS-II |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-11-04 |
| Detector | DECTRIS EIGER2 XE 16M |
| Wavelength(s) | 0.9786 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.984, 92.674, 108.548 |
| Unit cell angles | 90.00, 94.18, 90.00 |
Refinement procedure
| Resolution | 46.740 - 2.050 |
| R-factor | 0.212 |
| Rwork | 0.210 |
| R-free | 0.25070 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.523 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (1.21.2_5419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.000 | 2.090 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.139 | 0.736 |
| Rmeas | 0.158 | 0.918 |
| Rpim | 0.074 | 0.539 |
| Number of reflections | 57450 | 2747 |
| <I/σ(I)> | 10.86 | 1.06 |
| Completeness [%] | 99.5 | 95.9 |
| Redundancy | 4.1 | 2.4 |
| CC(1/2) | 0.988 | 0.484 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 289 | 0.18 M Ammonium Sulfate, 0.09 M Tris:HCl, 22.5% (w/v) PEG3350, 0.01 M Zinc Chloride |
