3KYO
Crystal structure of HLA-G presenting KLPAQFYIL peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-12-12 |
Detector | MARMOSAIC 300 mm CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 58.606, 85.982, 111.570 |
Unit cell angles | 90.00, 95.61, 90.00 |
Refinement procedure
Resolution | 43.000 - 1.700 |
R-factor | 0.18382 |
Rwork | 0.182 |
R-free | 0.22645 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ydp |
RMSD bond length | 0.022 |
RMSD bond angle | 1.888 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.000 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.082 | 0.589 |
Number of reflections | 119833 | |
<I/σ(I)> | 33.4 | 2.9 |
Redundancy | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 277 | 16% PEG 3350, 0.2M potassium formate, 0.1M HEPES, 10mM cobalt chloride, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K |