2E33
Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-07-23 |
| Detector | Bruker DIP-6040 |
| Wavelength(s) | 0.9000 |
| Spacegroup name | P 4 3 2 |
| Unit cell lengths | 148.314, 148.314, 148.314 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.700 |
| R-factor | 0.2198 |
| Rwork | 0.216 |
| R-free | 0.28807 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1umh |
| RMSD bond length | 0.026 |
| RMSD bond angle | 2.508 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 149.100 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.078 | 0.325 |
| Number of reflections | 15839 | |
| <I/σ(I)> | 13.9 | 5.2 |
| Completeness [%] | 99.4 | 97.9 |
| Redundancy | 11.8 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 2.0% (v/v) PEG 400, 0.1M HEPES, 2.1M ammonium sulfate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
