6CQJ
Crystal structure of DR1 presenting the RQ13 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-06-17 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.984 |
Spacegroup name | P 1 |
Unit cell lengths | 68.684, 82.017, 83.050 |
Unit cell angles | 61.56, 88.20, 86.47 |
Refinement procedure
Resolution | 47.960 - 2.750 |
R-factor | 0.2 |
Rwork | 0.197 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4mdo |
RMSD bond length | 0.010 |
RMSD bond angle | 1.170 |
Data reduction software | XDS |
Data scaling software | Aimless |
Refinement software | BUSTER (2.10.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.960 | 2.860 |
High resolution limit [Å] | 2.750 | 2.750 |
Rpim | 0.076 | 0.417 |
Number of reflections | 40739 | 4564 |
<I/σ(I)> | 8.1 | |
Completeness [%] | 98.6 | |
Redundancy | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 295 | HEPES pH 7.5, Na acetate, PEG 4000 |