Abstract
Pentaerythritol tetranitrate (PETN) reductase of Enterobacter cloacae PB2, a flavoprotein involved in the biodegradation of the explosive PETN, ethylene glycol dinitrate (EGDN) and glycerol trinitrate (GTN), was purified from an overexpressing strain of E. coli and crystallized at 293 K using the sitting-drop vapour-diffusion method. Diffraction data can be seen at 1.8 Å. The primitive orthorhombic cell has a monomer in the asymmetric unit. Preliminary molecular-replacement calculations have been performed using a search model based on Old Yellow enzyme.
Original language | English |
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Pages (from-to) | 675-677 |
Number of pages | 2 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 54 |
Issue number | 4 |
DOIs | |
Publication status | Published - 1 Jul 1998 |