1LDD
Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 170 |
| Detector technology | CCD |
| Wavelength(s) | 0.9747 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.700, 72.900, 79.800 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.000 |
| R-factor | 0.205 * |
| Rwork | 0.205 |
| R-free | 0.26600 |
| Structure solution method | MAD |
| RMSD bond length | 0.012 * |
| RMSD bond angle | 1.400 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXS |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 30.000 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.052 * |
| Total number of observations | 120747 * |
| Number of reflections | 40867 |
| Completeness [%] | 97.9 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 4 * | PEG4K, 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 | 80 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 18.5 (%) | |
| 3 | 1 | reservoir | 0.16 (M) | ||
| 4 | 1 | reservoir | Tris | 0.1 (M) | pH8.5 |






