1I1F
Crystal structure of human class i mhc (hla-a2.1) complexed with beta 2-microglobulin and hiv-rt variant peptide i1y
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1997-12 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 1 |
Unit cell lengths | 49.574, 62.970, 74.559 |
Unit cell angles | 82.09, 76.47, 77.78 |
Refinement procedure
Resolution | 15.000 - 2.800 |
R-factor | 0.274 |
Rwork | 0.260 |
R-free | 0.31500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hhh |
RMSD bond length | 0.009 * |
RMSD bond angle | 2.493 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE (IN CCP4) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.110 | 0.320 |
Total number of observations | 148065 * | |
Number of reflections | 21030 | |
<I/σ(I)> | 13.2 | 4.2 |
Completeness [%] | 99.2 | 98.6 |
Redundancy | 7 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | drop consists of 1:1 mixture of well and protein solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protease | 10 (mg/ml) | |
2 | 1 | drop | MES | 25 (mM) | |
3 | 1 | reservoir | PEG8000 | 20 (%) | |
4 | 1 | reservoir | MES | 25 (mM) |