5EMZ
Crystal structure of K48-linked diubiquitin with F45W mutation in the proximal unit
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-10-22 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.00 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 58.870, 78.920, 91.510 |
| Unit cell angles | 90.00, 97.93, 90.00 |
Refinement procedure
| Resolution | 43.676 - 1.660 |
| R-factor | 0.1729 |
| Rwork | 0.171 |
| R-free | 0.20890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3m3j |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.923 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 43.680 |
| High resolution limit [Å] | 1.660 |
| Number of reflections | 46959 |
| <I/σ(I)> | 7.94 |
| Completeness [%] | 95.8 |
| Redundancy | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 298 | LiSO Tris PEG-3350 |
