4N9Z
Crystal structure of mouse poly(ADP-ribose) glycohydrolase (PARG) catalytic domain mutant E749Q
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-06-02 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 66.915, 91.283, 102.522 |
Unit cell angles | 90.00, 91.20, 90.00 |
Refinement procedure
Resolution | 29.880 - 1.900 |
R-factor | 0.1921 |
Rwork | 0.190 |
R-free | 0.23030 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4fc2 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.345 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.880 | 1.960 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.110 | |
Number of reflections | 95128 | |
Completeness [%] | 98.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 277 | 0.2M (NH4)2SO4, 16% PEG3,350, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K |