5A00
Structure of human PARP1 catalytic domain bound to an isoindolinone inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 49.083, 89.392, 193.187 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.750 |
R-factor | 0.20856 |
Rwork | 0.205 |
R-free | 0.27963 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.099 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.900 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmerge | 0.080 | 0.660 |
Number of reflections | 11464 | |
<I/σ(I)> | 15.9 | 3 |
Completeness [%] | 99.8 | 99.8 |
Redundancy | 7.1 | 7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 277 | 2M AMMONIUM SULFATE, 2% PEG400 0.1 M TRIS PH 8.0 TEMPERATURE 277K - |