1B16
ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS TERNARY COMPLEX WITH NAD-3-PENTANONE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X31 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-11-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 66.800, 53.000, 70.500 |
| Unit cell angles | 90.00, 107.20, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.400 |
| Rwork | 0.184 |
| R-free | 0.21300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1a4u |
| RMSD bond length | 0.009 * |
| RMSD bond angle | 1.890 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.430 |
| High resolution limit [Å] | 1.320 | 1.320 |
| Rmerge | 0.060 | 0.400 |
| Total number of observations | 262892 * | |
| Number of reflections | 103695 | |
| <I/σ(I)> | 3 | 3 |
| Completeness [%] | 94.0 | 94 |
| Redundancy | 3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8.6 * | 277 * | PROTEIN WAS CRYSTALLIZED FROM 28% PEG 2000, 0.2 M CACL2, 0.1 M TRIS-HCL, PH= 7.5, 1MM NAD+, 1% 3-PENTANONE, 4 C. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | |
| 3 | 1 | drop | isopropanol | 1 (%) | |
| 4 | 1 | drop | dithiothreitol | 2 (mM) | |
| 5 | 1 | reservoir | PEG2000 | 28 (%) | |
| 6 | 1 | reservoir | 0.2 (M) | ||
| 7 | 1 | reservoir | Tris-HCl | 0.1 (M) |
