1QLF
MHC CLASS I H-2DB COMPLEXED WITH GLYCOPEPTIDE K3G
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 61.073, 58.272, 77.146 |
Unit cell angles | 90.00, 108.57, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.650 |
R-factor | 0.204 |
Rwork | 0.204 |
R-free | 0.26700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ce6 |
RMSD bond length | 0.007 |
RMSD bond angle | 24.600 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS (0.5) |
Refinement software | CNS (0.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 2.730 |
High resolution limit [Å] | 2.650 | 2.650 |
Rmerge | 0.060 * | 0.176 * |
Number of reflections | 14363 | |
Completeness [%] | 97.0 | 95.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.5 * | 4 * | pH 5.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | peptide complex | 10 (mg/ml) | |
2 | 1 | drop | Tris buffered saline | ||
3 | 1 | reservoir | PEG6000 | 15-23 (%) | |
4 | 1 | reservoir | ammonium sulfate | 100 (mM) | |
5 | 1 | reservoir | MES | 100 (mM) |