1UXH
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 BM1A |
| Synchrotron site | ESRF |
| Beamline | BM1A |
| Temperature [K] | 110 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 149.790, 149.790, 111.264 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.100 |
| R-factor | 0.235 |
| Rwork | 0.235 |
| R-free | 0.26200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1guy |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.260 |
| 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 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.137 | 0.520 |
| Number of reflections | 73640 | |
| <I/σ(I)> | 18.8 | 3.2 |
| Completeness [%] | 92.1 | 80.9 |
| Redundancy | 12.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 20-40% PEG400, 100MM NASUCCINATE, PH 6.5 |
