3RIS
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 | 2008-06-30 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.03303 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 87.393, 41.670, 138.729 |
| Unit cell angles | 90.00, 89.93, 90.00 |
Refinement procedure
| Resolution | 41.700 - 2.398 |
| R-factor | 0.20403 |
| Rwork | 0.201 |
| R-free | 0.25827 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.045 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.490 |
| High resolution limit [Å] | 2.398 | 2.398 |
| Rmerge | 0.084 | 0.648 |
| Number of reflections | 39644 | |
| <I/σ(I)> | 14.7 | 1.6 |
| Completeness [%] | 99.1 | 92.1 |
| Redundancy | 3.5 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 1.6 M Ammonium sulfate, 0.1 M Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
