2PU3
Structural adaptation of endonuclease I from the cold-adapted and halophilic bacterium Vibrio salmonicida
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 | 2005-05-02 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0707 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.078, 44.948, 51.746 |
| Unit cell angles | 90.00, 92.66, 90.00 |
Refinement procedure
| Resolution | 33.920 - 1.500 |
| R-factor | 0.167 |
| Rwork | 0.166 |
| R-free | 0.18500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ouo |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.142 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.923 | 1.580 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.047 | 0.074 |
| Number of reflections | 30823 | |
| <I/σ(I)> | 9.4 | 14 |
| Completeness [%] | 99.3 | 97.6 |
| Redundancy | 4 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.2 | 298 | 30 % PEG 3350, 0.1 M Tris, 0.25 M sodium acetate, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
