1FLG
CRYSTAL STRUCTURE OF THE QUINOPROTEIN ETHANOL DEHYDROGENASE FROM PSEUDOMONAS AERUGINOSA
Replaces: 1EEEExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
| Synchrotron site | EMBL/DESY, Hamburg |
| Beamline | X31 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1989-06-29 |
| Detector | MARRESEARCH |
| Spacegroup name | H 3 |
| Unit cell lengths | 159.400, 159.400, 130.950 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 12.500 - 2.600 |
| R-factor | 0.192 * |
| Rwork | 0.192 |
| R-free | 0.27400 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 5.000 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((AGROVATA) |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.700 | 2.700 |
| High resolution limit [Å] | 2.520 | 2.600 |
| Rmerge | 0.126 * | 0.360 * |
| Total number of observations | 109117 * | |
| Number of reflections | 41300 | |
| <I/σ(I)> | 15 | |
| Completeness [%] | 94.2 | 98.8 |
| Redundancy | 2.7 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | Stezowski, J.J., (1989) J. Mol. Biol., 205, 617. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | ethanol dehydrogenase | 0.005ml | |
| 2 | 1 | drop | protein | 2 (mg/ml) | |
| 3 | 1 | drop | glycine-NaOH | 4.5 (mM) | |
| 4 | 1 | drop | 1.5 (mM) | ||
| 5 | 1 | drop | 0.02 (%(w/v)) | ||
| 6 | 1 | reservoir | PEG1550 | 22.5 (%(v/v)) | |
| 7 | 1 | reservoir | 0.01 (%) | ||
| 8 | 1 | reservoir | 3 (mM) | ||
| 9 | 1 | reservoir | glycine-NaOH | 50 (mM) |
