5URO
Structure of a soluble epoxide hydrolase identified in Trichoderma reesei
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1) |
| Synchrotron site | PETRA III, EMBL c/o DESY |
| Beamline | P13 (MX1) |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-08-15 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.97625 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 51.427, 78.281, 87.372 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.320 - 1.701 |
| R-factor | 0.1841 |
| Rwork | 0.183 |
| R-free | 0.21060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ans |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER (2.5.6) |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 44.320 |
| High resolution limit [Å] | 1.701 |
| Number of reflections | 74551 |
| <I/σ(I)> | 1.34 |
| Completeness [%] | 99.0 |
| Redundancy | 12.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 298 | PEG 400 |
