6MP1
Crystal structures of the murine class I major histocompatibility complex H-2Db in complex with the mutant TRP1-K8 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-08-05 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.97918 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.569, 68.329, 117.787 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.005 - 2.211 |
R-factor | 0.2111 |
Rwork | 0.209 |
R-free | 0.24420 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4huu |
RMSD bond length | 0.003 |
RMSD bond angle | 0.641 |
Data reduction software | XDS (20170601) |
Data scaling software | XSCALE (20170601) |
Phasing software | PHASER |
Refinement software | PHENIX ((1.13_2998: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.016 | 2.290 |
High resolution limit [Å] | 2.211 | 2.211 |
Rmerge | 0.114 | 1.711 |
Rmeas | 0.120 | 1.825 |
Number of reflections | 21851 | |
<I/σ(I)> | 13.82 | 0.89 |
Completeness [%] | 99.4 | |
Redundancy | 9.6 | |
CC(1/2) | 0.998 | 0.406 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 295 | 30% PEG-1500, 100 mM MIB buffer, pH 7.0 |