4IQY
Crystal structure of the human protein-proximal ADP-ribosyl-hydrolase MacroD2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2010-09-18 |
| Detector | PSI PILATUS 6M |
| Wavelength(s) | 0.97633 |
| Spacegroup name | P 1 |
| Unit cell lengths | 40.713, 49.883, 66.972 |
| Unit cell angles | 69.82, 72.35, 86.08 |
Refinement procedure
| Resolution | 46.783 - 1.550 |
| R-factor | 0.1597 |
| Rwork | 0.158 |
| R-free | 0.18700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2x47 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.208 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.780 | 1.550 |
| High resolution limit [Å] | 1.470 | 1.470 |
| Rmerge | 0.045 | 0.416 |
| Number of reflections | 72823 | |
| <I/σ(I)> | 10.4 | 2 |
| Completeness [%] | 90.9 | 87.8 |
| Redundancy | 2 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 18% PEG3350, 0.1M HEPES, 0.1M MgFormate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
