6P2F
Structure of a nested set of N-terminally extended MHC I-peptides provides novel insights into antigen processing and presentation
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2018-10-04 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.845, 81.919, 111.060 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.215 - 1.482 |
| R-factor | 0.216 |
| Rwork | 0.214 |
| R-free | 0.24520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1agb |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.353 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.215 | 1.530 |
| High resolution limit [Å] | 1.480 | 1.480 |
| Rmerge | 0.070 | 0.580 |
| Number of reflections | 76357 | 7231 |
| <I/σ(I)> | 11.67 | |
| Completeness [%] | 98.8 | |
| Redundancy | 5.6 | |
| CC(1/2) | 0.795 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 0.2 M ammonium sulfate, 18% PEG4000, 0.1 M sodium cacodylate, pH 5.7 |
