Crystallization and preliminary diffraction studies of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2

P C E Moody, N Shikotra, C E French, N C Bruce, N S Scrutton

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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 Angstrom. 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 languageEnglish
Pages (from-to)675-677
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume54
Issue numberPt 4
DOIs
Publication statusPublished - 1 Jul 1998

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