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 |