1HQR
CRYSTAL STRUCTURE OF A SUPERANTIGEN BOUND TO THE HIGH-AFFINITY, ZINC-DEPENDENT SITE ON MHC CLASS II
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-03-15 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.978 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 61.827, 111.950, 216.617 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 100.000 - 3.200 |
R-factor | 0.224 |
Rwork | 0.224 |
R-free | 0.28800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 25.700 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.4) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 3.300 |
High resolution limit [Å] | 3.200 | 3.200 |
Rmerge | 0.110 | 0.362 |
Total number of observations | 141485 * | |
Number of reflections | 11585 | |
<I/σ(I)> | 12.4 | 5.1 |
Completeness [%] | 90.2 | 92.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298.15 | drop consists of equal amounts of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 1.8 (M) | |
3 | 1 | reservoir | PEG400 | 5 (%) | |
4 | 1 | reservoir | sodium cacodylate | 0.1 (M) | |
5 | 1 | reservoir | 5 (mM) |