1UR5
Stabilization of a Tetrameric Malate Dehydrogenase by Introduction of a Disulfide Bridge 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 31 2 1 |
| Unit cell lengths | 105.575, 105.575, 102.531 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 25.000 - 1.750 |
| R-factor | 0.19 |
| Rwork | 0.190 |
| R-free | 0.22300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1guy |
| RMSD bond length | 0.004 * |
| RMSD bond angle | 21.300 * |
| 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 | 0.129 | 0.457 |
| Total number of observations | 674394 * | |
| Number of reflections | 66684 | |
| <I/σ(I)> | 22.8 | 4.6 |
| Completeness [%] | 96.6 | 89 |
| Redundancy | 10.1 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4.5 | 288 * | 15% PEG400, 100MM NAAC, PH 4.5, 40MM CD2+ |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | reservoir | PEG400 | 15 (%) | |
| 3 | 1 | reservoir | sodium acetate | 100 (mM) | pH4.5 |
| 4 | 1 | reservoir | 40 (mM) |
