8P43
Structure of the MHC class Ib molecule Qa-1b in complex with Q001 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX IV BEAMLINE BioMAX |
Synchrotron site | MAX IV |
Beamline | BioMAX |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-05-22 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.97625 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 59.560, 72.797, 96.515 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.690 - 2.430 |
R-factor | 0.1939 |
Rwork | 0.191 |
R-free | 0.24700 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 0.986 |
Data reduction software | AutoProcess |
Data scaling software | TRUNCATE |
Phasing software | PHENIX |
Refinement software | PHENIX (1.19.1_4122) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.690 | 2.517 |
High resolution limit [Å] | 2.430 | 2.430 |
Rmerge | 0.034 | 0.255 |
Rmeas | 0.048 | 0.360 |
Rpim | 0.034 | 0.255 |
Number of reflections | 16416 | 1605 |
<I/σ(I)> | 13.23 | |
Completeness [%] | 99.9 | 99.88 |
Redundancy | 2 | 2 |
CC(1/2) | 0.999 | 0.895 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 8% PEG4000, 0.1M sodium acetate (pH 5.7) and 10 mM NiCl2 |