1UXG
Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 110 |
Detector technology | CCD |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 149.832, 149.832, 110.580 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.900 |
R-factor | 0.248 |
Rwork | 0.248 |
R-free | 0.27000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1guy |
RMSD bond length | 0.006 |
RMSD bond angle | 1.240 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.980 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.058 | 0.530 |
Number of reflections | 81226 | |
<I/σ(I)> | 23.6 | 2.9 |
Completeness [%] | 91.2 | 80.1 |
Redundancy | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 20-40% PEG400, 100MM NASUCCINATE PH 6.5 |