6ISU
Crystal structure of Lys27-linked di-ubiquitin in complex with its selective interacting protein UCHL3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17B1 |
| Synchrotron site | SSRF |
| Beamline | BL17B1 |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2018-01-10 |
| Detector | BRUKER SMART 6000 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 91.407, 94.204, 91.178 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.850 - 1.866 |
| R-factor | 0.2121 |
| Rwork | 0.209 |
| R-free | 0.26440 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1xd3 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.861 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.13_2998: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.850 | 1.933 |
| High resolution limit [Å] | 1.866 | 1.866 |
| Number of reflections | 29404 | |
| <I/σ(I)> | 31.32 | |
| Completeness [%] | 88.8 | |
| Redundancy | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291.15 | 18% PEG 3350 (w/v), 400 mM Ca(AC)2 |
