1UXJ
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 | EMBL/DESY, HAMBURG BEAMLINE X31 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X31 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 105.247, 105.247, 102.196 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.000 - 1.750 |
R-factor | 0.177 |
Rwork | 0.177 |
R-free | 0.21100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1guy |
RMSD bond length | 0.005 |
RMSD bond angle | 1.160 |
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] | 25.000 | 1.810 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.049 | 0.430 |
Number of reflections | 61743 | |
<I/σ(I)> | 18.1 | 2 |
Completeness [%] | 93.2 | 79.7 |
Redundancy | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.5 | 10-20% PEG400, 100MM NAACETATE, PH 4.5, 40MM CDCL2 |