1P7Q
Crystal Structure of HLA-A2 Bound to LIR-1, a Host and Viral MHC Receptor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.3 |
Synchrotron site | ALS |
Beamline | 5.0.3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-10-28 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.992 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 113.740, 113.740, 89.460 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 * - 3.400 |
R-factor | 0.218 |
Rwork | 0.218 |
R-free | 0.31000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB entries 1G0X and 1AKJ |
RMSD bond length | 0.021 * |
RMSD bond angle | 1.850 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.610 |
High resolution limit [Å] | 3.400 | 3.400 |
Rmerge | 0.180 | 0.505 |
Total number of observations | 61195 * | |
Number of reflections | 9493 | 928 * |
<I/σ(I)> | 11.7 | 3.8 |
Completeness [%] | 99.9 | 100 |
Redundancy | 6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | PEG 4000, Sodium Acetate, Tris, L-Cysteine, Triton X-100, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 14.5 (mg/ml) | |
2 | 1 | drop | sodium acetate | 0.2 (M) | |
3 | 1 | drop | Tris | 0.1 (M) | pH8.5 |
4 | 1 | drop | PEG4000 | 30 (%(w/v)) | |
5 | 1 | reservoir | sodium acetate | 0.2 (M) | |
6 | 1 | reservoir | Tris | 0.1 (M) | pH8.5 |
7 | 1 | reservoir | PEG4000 | 30 (%(w/v)) | |
8 | 1 | reservoir | L-cysteine | 20 (mM) | |
9 | 1 | reservoir | TritonX-100 | 1.8 (mM) |