3P43
Structure and Activities 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) | 1.1 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 30.368, 60.166, 76.471 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.236 - 2.100 |
| R-factor | 0.2086 |
| Rwork | 0.203 |
| R-free | 0.25720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n9b |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.950 |
| 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] | 38.236 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.465 | |
| Number of reflections | 8606 | |
| <I/σ(I)> | 11.12 | 2.74 |
| Completeness [%] | 97.5 | 97.2 |
| Redundancy | 4.9 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | vapor-diffusion, sitting-drop setups with 1:1 mixtures of protein solution containing 0.5 mM Mba and 2mM MnCl2 and reservoir solution containing PEG 4000 (32%), 0.18 M MgCl2, 2.5% 1,4-dioxane, 0.1 M Tris-HCl pH 7.5, temperature 298K, VAPOR DIFFUSION, SITTING DROP |
