3RII
Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-27 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97948 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 45.395, 99.034, 48.145 |
| Unit cell angles | 90.00, 96.39, 90.00 |
Refinement procedure
| Resolution | 41.054 - 2.001 |
| R-factor | 0.1774 |
| Rwork | 0.175 |
| R-free | 0.22220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.658 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.122 | 0.462 |
| Number of reflections | 27641 | |
| <I/σ(I)> | 12.9 | 2.8 |
| Completeness [%] | 96.8 | 93.1 |
| Redundancy | 6 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 30% PEG 3350, 0.1M MgCl2, 0.1M Tris-HCl, pH 8.5, 3% Trimethyl amino oxide, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
