1GV0
Structural Basis for Thermophilic Protein Stability: Structures of Thermophilic and Mesophilic Malate Dehydrogenases
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 114.320, 149.420, 97.730 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.900 - 2.500 |
| R-factor | 0.221 |
| Rwork | 0.221 |
| R-free | 0.27500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | MDH WITH PDB-CODE 1GUZ |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.150 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | EPMR |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.800 | 2.640 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.070 | 0.254 |
| Total number of observations | 117908 * | |
| Number of reflections | 28459 | |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.4 * | 15 * | 20MG/ML,50MMTRIS-HCL,PH7.4,55%MPD, 100MMHEPES,PH7.5., pH 7.50 |
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 | MPD | 53 (%(v/v)) | |
| 4 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
