6P2C
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-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 80 |
Detector technology | CCD |
Collection date | 2019-02-08 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.790, 81.767, 111.871 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.602 - 1.396 |
R-factor | 0.1975 |
Rwork | 0.196 |
R-free | 0.20980 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1agb |
RMSD bond length | 0.005 |
RMSD bond angle | 1.021 |
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] | 37.610 | 1.450 |
High resolution limit [Å] | 1.390 | 1.400 |
Rmerge | 0.060 | 0.390 |
Number of reflections | 93207 | 9169 |
<I/σ(I)> | 19.1 | |
Completeness [%] | 99.9 | |
Redundancy | 9.2 | |
CC(1/2) | 0.965 |
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 |