4FC2
Crystal structure of mouse poly(ADP-ribose) glycohydrolase (PARG) catalytic domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 95 |
Detector technology | CCD |
Collection date | 2012-03-31 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9774 |
Spacegroup name | P 1 |
Unit cell lengths | 67.141, 90.401, 104.696 |
Unit cell angles | 81.64, 88.41, 89.36 |
Refinement procedure
Resolution | 50.000 - 1.910 |
R-factor | 0.1759 |
Rwork | 0.174 |
R-free | 0.21440 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.123 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.980 |
High resolution limit [Å] | 1.910 | 1.910 |
Number of reflections | 173052 | |
Completeness [%] | 92.1 | 54.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 277 | 0.2M (NH4)2SO4, 16% PEG3,350, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |