7M3Q
Structure of the Smurf2 HECT Domain with a High Affinity Ubiquitin Variant (UbV)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-10-14 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 201.530, 72.068, 48.813 |
| Unit cell angles | 90.00, 94.61, 90.00 |
Refinement procedure
| Resolution | 67.830 - 2.500 |
| R-factor | 0.2045 |
| Rwork | 0.203 |
| R-free | 0.23490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ZVD and Swiss Model of Ubiquitin Variant |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.144 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 67.830 | 2.550 |
| High resolution limit [Å] | 2.450 | 2.450 |
| Rmerge | 0.089 | 0.675 |
| Number of reflections | 24895 | 2871 |
| <I/σ(I)> | 8.8 | 2.2 |
| Completeness [%] | 97.1 | 99.2 |
| Redundancy | 3.3 | 3.5 |
| CC(1/2) | 0.982 | 0.478 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 298 | 1.5 M Ammonium Sulphate and 100 mM MES pH 6.0. Trypsin was added to the protein complex at a final concentration of 10 microgram per mL |
