3RJ5
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 | C 1 2 1 |
| Unit cell lengths | 149.300, 53.870, 76.750 |
| Unit cell angles | 90.00, 103.60, 90.00 |
Refinement procedure
| Resolution | 31.250 - 1.450 |
| R-factor | 0.2065 |
| Rwork | 0.206 |
| R-free | 0.23921 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1a4u |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.151 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 31.250 | 1.530 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.118 | 0.497 |
| Number of reflections | 103038 | |
| <I/σ(I)> | 7.4 | 1.2 |
| Completeness [%] | 97.9 | 90.3 |
| Redundancy | 3.5 | 3 |
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 |
