1UXK
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 | 105.405, 105.405, 102.305 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.000 - 1.800 |
R-factor | 0.178 |
Rwork | 0.178 |
R-free | 0.21400 |
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 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.043 | 0.530 |
Number of reflections | 55441 | |
<I/σ(I)> | 19.5 | 2.1 |
Completeness [%] | 90.7 | 68 |
Redundancy | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.5 | 10-20% PEG400, NA ACETATE PH 4.5, 40MM CDCL2 |