1GV1
Structural Basis for Thermophilic Protein Stability: Structures of Thermophilic and Mesophilic Malate Dehydrogenases
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 64.425, 85.824, 117.498 |
| Unit cell angles | 90.00, 104.61, 90.00 |
Refinement procedure
| Resolution | 19.920 - 2.500 |
| R-factor | 0.216 |
| Rwork | 0.216 |
| R-free | 0.30500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | MDH WITH PDB-CODE 1GUZ |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.260 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS (1.0) |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 * | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.079 | 0.251 |
| Total number of observations | 388140 * | |
| Number of reflections | 37824 | |
| <I/σ(I)> | 11 | 2.5 |
| Completeness [%] | 92.5 | 84.1 |
| Redundancy | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.4 * | ~20 MG/ML, 50 MM TRIS-HCL, PH 7.4, 40 % PEG-MME5000, 100 MM |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | pH7.4 |
| 3 | 1 | reservoir | PEG5000 MME | 40 (%) | |
| 4 | 1 | reservoir | sodium succinate | 100 (mM) | pH6.0 |
