5LP8
Crystal structure of an asymmetric dimer of the ubiquitin ligase HUWE1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-02-27 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | P 63 |
| Unit cell lengths | 177.464, 177.464, 106.259 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 46.150 - 2.700 |
| R-factor | 0.195 |
| Rwork | 0.194 |
| R-free | 0.22500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3h1d |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.743 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.150 | 2.780 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.058 | 0.349 |
| Number of reflections | 52053 | |
| <I/σ(I)> | 16.2 | 2.6 |
| Completeness [%] | 99.4 | 98.5 |
| Redundancy | 4.2 | 2.89 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | Hepes pH 7, PEG20000 |






