1GUY
Structural Basis for Thermophilic Protein Stability: Structures of Thermophilic and Mesophilic Malate Dehydrogenases
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 106.670, 106.670, 103.990 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.870 - 2.200 |
| R-factor | 0.174 |
| Rwork | 0.174 |
| R-free | 0.19700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | MODIFICATION OF PDB ENTRY 1LDB |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.130 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.330 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.124 | 0.284 |
| Total number of observations | 80712 * | |
| Number of reflections | 35062 | |
| Completeness [%] | 99.7 | 87.1 |
| Redundancy | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4.6 | 5-15% PEG400, 100 MM NAAC, PH 4.6, 40MM 5-15% PEG400, 100 MM NAAC, PH 4.6, 40MM CDAC |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | PEG400 | 5-15 (%) | |
| 2 | 1 | drop | sodium acetate | 100 (mM) | pH4.6 |
| 3 | 1 | drop | cadmium acetate | 40 (mM) | |
| 4 | 1 | reservoir | PEG400 | 15 (%) | |
| 5 | 1 | reservoir | sodium acetate | 100 (mM) | pH4.6 |
