9O4M
Crystal structure of Ubiquitin Carboxy Terminal Hydrolase L1 Q209C mutant covalently crosslinked to ubiquitin genetically encoded with N6-(6-bromohexanoyl)-L-lysine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-04-10 |
| Detector | DECTRIS EIGER2 R 4M |
| Wavelength(s) | 1.54184 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 93.867, 93.867, 140.330 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.930 - 2.000 |
| R-factor | 0.226 |
| Rwork | 0.224 |
| R-free | 0.26200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.439 |
| Data reduction software | CrysalisPro |
| Data scaling software | CrysalisPro |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 140.330 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.835 | |
| Number of reflections | 48911 | 4906 |
| <I/σ(I)> | 16.91 | 1.02 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 10.3 | 9.8 |
| CC(1/2) | 0.998 | 0.926 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 2.1 M DL-Malic acid |
