1S0X
Crystal structure of the human RORalpha ligand binding domain in complex with cholesterol sulfate at 2.2A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-10-17 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9200 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.400, 49.900, 60.700 |
| Unit cell angles | 90.00, 97.80, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.19734 |
| Rwork | 0.197 |
| R-free | 0.21900 * |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 1n83 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.410 * |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((TRUNCATE)) |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.079 | |
| Total number of observations | 57993 * | |
| Number of reflections | 16541 | |
| <I/σ(I)> | 16.2 | |
| Completeness [%] | 99.7 | 99.4 |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 4 * | PEG 4000, magnesium chloride, Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 17.6 (mg/ml) | |
| 2 | 1 | reservoir | 0.2 (M) | ||
| 3 | 1 | reservoir | PEG4000 | 16 (M) | |
| 4 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.5 |
