1NWW
Limonene-1,2-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 | 1999-02-06 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.931 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.548, 47.652, 129.701 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.200 |
| R-factor | 0.14822 |
| Rwork | 0.147 |
| R-free | 0.17200 * |
| Structure solution method | SAD |
| Starting model (for MR) | Model from structure solution using SAD on Se-Met labelled protein. SAD data collected at ESRF beamline ID14-1 at 0.934 A wavelength. |
| RMSD bond length | 0.025 * |
| RMSD bond angle | 2.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SnB (V. 2.1) |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 64.600 | 1.210 |
| High resolution limit [Å] | 1.200 | 1.200 |
| Rmerge | 0.063 * | 0.272 * |
| Number of reflections | 88916 | |
| <I/σ(I)> | 28.2 | 3.5 |
| Completeness [%] | 99.7 | 94.1 |
| Redundancy | 4.1 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 * | 4 * | PEG 6000, LiCl, MES, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12.8 (mg/ml) | |
| 2 | 1 | drop | HEPES | 10 (mM) | pH7.0 |
| 3 | 1 | reservoir | PEG6000 | 30 (%) | |
| 4 | 1 | reservoir | 1 (M) | ||
| 5 | 1 | reservoir | MES | 0.1 (M) | pH6.0 |
