3OLM
Structure and Function of a Ubiquitin Binding Site within the Catalytic Domain of a HECT Ubiquitin Ligase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-28 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.03326 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 161.570, 50.331, 79.684 |
| Unit cell angles | 90.00, 116.72, 90.00 |
Refinement procedure
| Resolution | 42.085 - 2.495 |
| R-factor | 0.2227 |
| Rwork | 0.220 |
| R-free | 0.27160 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1nd7 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.488 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Number of reflections | 14422 | |
| Completeness [%] | 75.2 | 33.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9 | 293 | 13.5% PEG 4000, 0.2M magnesium chloride, 0.1M Tris-HCl pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
