2GFO
Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-terminal Hydrolase 8
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-03-09 |
Detector | SBC-3 |
Wavelength(s) | 0.97896 |
Spacegroup name | P 61 |
Unit cell lengths | 67.173, 67.173, 194.458 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 18.200 - 2.000 |
R-factor | 0.17056 |
Rwork | 0.168 |
R-free | 0.21023 |
Structure solution method | SAD |
RMSD bond length | 0.015 |
RMSD bond angle | 1.498 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.200 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.085 | |
Number of reflections | 33281 | |
<I/σ(I)> | 20.03 | |
Completeness [%] | 99.4 | 99.9 |
Redundancy | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.3 | 298 | 18% PEG3350; 0.1 M bis-Tris, pH 6.3, 0.2 M KSCN, 1 mM DTT., VAPOR DIFFUSION, HANGING DROP, temperature 298, temperature 298.0K |