6UPS
Crystal structure of the deubiquitylase domain from the Orientia tsutsugamushi protein OTT_1962 (OtDUB)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-E |
Synchrotron site | APS |
Beamline | 21-ID-E |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-06-10 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.98 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 114.787, 43.093, 58.244 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.670 - 2.000 |
R-factor | 0.2092 |
Rwork | 0.208 |
R-free | 0.23710 |
Structure solution method | SAD |
RMSD bond length | 0.013 |
RMSD bond angle | 1.468 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELXD |
Refinement software | REFMAC (5.8.0257) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.144 | 0.825 |
Number of reflections | 18794 | 1895 |
<I/σ(I)> | 10.6 | 1.6 |
Completeness [%] | 91.0 | 93.7 |
Redundancy | 4.3 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 0.2 M ammonium iodide, 20% (w/v) PEG 3350 |