3PRM
Structural analysis of a viral OTU domain protease from the Crimean-Congo Hemorrhagic Fever virus in complex with human ubiquitin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-10-31 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.978 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 60.462, 65.651, 133.133 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.480 - 2.300 |
R-factor | 0.2076 |
Rwork | 0.204 |
R-free | 0.26720 |
Structure solution method | SAD |
RMSD bond length | 0.018 |
RMSD bond angle | 1.642 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHENIX |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 66.570 | 2.340 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.072 | 0.322 |
Number of reflections | 23928 | |
Completeness [%] | 98.7 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 22-26% PEG 8000, 0.1 M Na cacodylate, 0.2 M Mg acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |