2YEU
Structural and functional insights of DR2231 protein, the MazG-like nucleoside triphosphate pyrophosphohydrolase from Deinococcus radiodurans, complex with Gd
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-04-16 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 67.820, 110.750, 165.980 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 92.060 - 2.000 |
R-factor | 0.19008 |
Rwork | 0.188 |
R-free | 0.23150 |
Structure solution method | SAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.017 |
RMSD bond angle | 1.526 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELX |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 83.000 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.110 | 0.450 |
Number of reflections | 85194 | |
<I/σ(I)> | 13.4 | 4.1 |
Completeness [%] | 100.0 | 100 |
Redundancy | 8.1 | 8.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 0.01M MAGNESIUM CHLORIDE, 0.05M SODIUM CACODYLATE PH6.0, 1M LITHIUM SULPHATE. |