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) |
