1QSF
STRUCTURE OF A6-TCR BOUND TO HLA-A2 COMPLEXED WITH ALTERED HTLV-1 TAX PEPTIDE Y8A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-01-13 |
Detector | ADSC |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 224.665, 48.460, 93.739 |
Unit cell angles | 90.00, 90.46, 90.00 |
Refinement procedure
Resolution | 25.000 - 2.800 |
Rwork | 0.245 |
R-free | 0.28600 |
RMSD bond length | 0.010 * |
RMSD bond angle | 1.700 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.063 | 0.215 |
Number of reflections | 21020 | |
<I/σ(I)> | 13.5 | |
Completeness [%] | 87.9 | 87.9 |
Redundancy | 2.2 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 6.5 * | 290 | seeding with hanging drop vapor diffusion; 50 mM MOPS, pH 7.0, 75 mM MgSO4 and 13% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 12 (mg/ml) | |
2 | 1 | 1 | HLA-A2/peptide complexes | ||
3 | 1 | 1 | MES | 10 (mM) | |
4 | 1 | 1 | 50 (mM) | ||
5 | 1 | 1 | EDTA | 0.5 (mM) |