3RJ9
Structure of alcohol dehydrogenase from Drosophila lebanonesis T114V mutant complexed with NAD+
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-09-27 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97245 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 62.318, 94.829, 139.009 |
| Unit cell angles | 90.00, 98.33, 90.00 |
Refinement procedure
| Resolution | 49.620 - 1.980 |
| R-factor | 0.20917 |
| Rwork | 0.208 |
| R-free | 0.25560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1a4u |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.294 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.000 |
| High resolution limit [Å] | 1.980 | 1.980 |
| Rmerge | 0.092 | 0.283 |
| Number of reflections | 104218 | |
| <I/σ(I)> | 9.5 | 8.1 |
| Completeness [%] | 95.6 | 88.5 |
| Redundancy | 2.7 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | 24.8% PEG (3350), 0.2M lithium sulfate, 0.1M Bis-Tris, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
