3HFW
Crystal Structure of human ADP-ribosylhydrolase 1 (hARH1)
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 |
| Collection date | 2008-01-01 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.8505 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.280, 52.790, 140.340 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.920 |
| R-factor | 0.15578 |
| Rwork | 0.155 |
| R-free | 0.18527 |
| Structure solution method | SAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.579 |
| Refinement software | REFMAC (5.5.0070) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.920 | 1.920 |
| Rmerge | 0.153 | 0.805 |
| Number of reflections | 26290 | |
| <I/σ(I)> | 29.7 | 3 |
| Completeness [%] | 95.4 | 71.1 |
| Redundancy | 29.9 | 9.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 150 mM Li-acetate, 25% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
