6TMO
Structure determination of an enhanced affinity TCR, a24b17, in complex with HLA-A*02:01 presenting a MART-1 peptide, EAAGIGILTV
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I02 |
Synchrotron site | Diamond |
Beamline | I02 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-01-30 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9795 |
Spacegroup name | P 43 |
Unit cell lengths | 121.490, 121.490, 82.680 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 54.330 - 2.100 |
R-factor | 0.1744 |
Rwork | 0.172 |
R-free | 0.20880 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3hgi |
RMSD bond length | 0.016 |
RMSD bond angle | 1.556 |
Data reduction software | xia2 |
Data scaling software | SCALA (3.3.15) |
Phasing software | PHASER (2.1.4) |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 54.332 | 54.332 | 2.150 |
High resolution limit [Å] | 2.100 | 9.390 | 2.100 |
Rmerge | 0.029 | 0.713 | |
Rmeas | 0.096 | 0.033 | 0.807 |
Rpim | 0.033 | 0.012 | 0.277 |
Total number of observations | 5911 | 42829 | |
Number of reflections | 69920 | 800 | 5110 |
<I/σ(I)> | 16 | 39.3 | 3.6 |
Completeness [%] | 99.4 | 95.8 | 99 |
Redundancy | 8.3 | 7.4 | 8.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 0.1 M HEPES pH 7.5 0.2 M Ammonium Sulphate 15 % PEG 4000 8.7% Glycerol |