3PT2
Structure of a viral OTU domain protease bound to Ubiquitin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-05-19 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.9796 |
Spacegroup name | P 62 2 2 |
Unit cell lengths | 146.010, 146.010, 58.140 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.793 - 2.500 |
R-factor | 0.1699 |
Rwork | 0.164 |
R-free | 0.22420 |
Structure solution method | SAD |
RMSD bond length | 0.006 |
RMSD bond angle | 0.906 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | PHENIX ((phenix.refine: 1.6.1_357)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 52.800 | 2.640 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.093 | 0.401 |
Number of reflections | 13116 | |
<I/σ(I)> | 13.1 | 5.2 |
Completeness [%] | 99.9 | 100 |
Redundancy | 7.1 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 294 | 27% PEG4000, 0.1 M sodium acetate, 0.21 M ammonium sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K |