1H5Q
Mannitol dehydrogenase from Agaricus bisporus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM1A |
| Synchrotron site | ESRF |
| Beamline | BM1A |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-07-15 |
| Detector | MAR scanner 345 mm plate |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 227.250, 124.850, 132.690 |
| Unit cell angles | 90.00, 118.54, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.500 |
| R-factor | 0.193 |
| Rwork | 0.193 |
| R-free | 0.20900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cyd |
| RMSD bond length | 0.007 * |
| RMSD bond angle | 1.360 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.580 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.063 | 0.295 |
| Number of reflections | 508943 | 173816 * |
| <I/σ(I)> | 11.8 | 3.1 |
| Completeness [%] | 98.4 | 97 |
| Redundancy | 2.7 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.5 | 20 * | 90 MM TRIS-HCL PH 7.5, 18% PEG4000, 9% ISOPROPANOL |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-20 (mg/ml) | |
| 2 | 1 | drop | NADP | 1 (mM) | |
| 3 | 1 | reservoir | Tris-HCl | 90 (mM) | pH7.5 |
| 4 | 1 | reservoir | PEG4000 | 18 (%) | |
| 5 | 1 | reservoir | isopropanol | 9 (%) |
