1QO7
Structure of Aspergillus niger epoxide hydrolase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-06-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 62.690, 89.320, 75.770 |
| Unit cell angles | 90.00, 105.37, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.800 |
| R-factor | 0.224 |
| Rwork | 0.224 |
| R-free | 0.23200 |
| Structure solution method | MAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 22.300 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS (0.5) |
| Refinement software | CNS (0.5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.300 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.073 | 0.321 |
| Total number of observations | 263931 * | |
| Number of reflections | 74416 | |
| <I/σ(I)> | 15 | 5 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 3.5 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.4 * | 277 * | 20% PEG6000, 0.1M MES BUFFER PH 6.0, 0.1M NAAC. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 17 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | EDTA | 1 (mM) | |
| 4 | 1 | drop | 20 (mM) | ||
| 5 | 1 | drop | sodium azide | 0.02 (%) | |
| 6 | 1 | reservoir | PEG6000 | 20 (%) | |
| 7 | 1 | reservoir | MES | 0.1 (M) | |
| 8 | 1 | reservoir | unbuffered sodium acetate | 0.1 (M) |
