3P4H
Structures of archaeal members of the LigD 3'-phosphoesterase DNA repair enzyme superfamily
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 130 |
| Detector technology | CCD |
| Collection date | 2010-06-02 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.95 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 27.769, 58.458, 33.180 |
| Unit cell angles | 90.00, 102.25, 90.00 |
Refinement procedure
| Resolution | 23.397 - 1.100 |
| R-factor | 0.1354 |
| Rwork | 0.132 |
| R-free | 0.16470 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n9b |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.406 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.120 |
| High resolution limit [Å] | 1.100 | 1.100 |
| Rmerge | 0.038 | 0.372 |
| Number of reflections | 40543 | |
| <I/σ(I)> | 42 | 2.07 |
| Completeness [%] | 96.5 | 90.8 |
| Redundancy | 5.1 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 298 | Crystallization was carried out in sitting-drop vapor-diffusion setups with 1:1 mixtures of protein solution containing 0.7 mM Cko and 1.8 mM MnCl2 and reservoir solution containing 20% PEG 3350 and 0.2 M Na2HPO4 , pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
