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Crystallization and preliminary diffraction studies of pentaerythritol tetranitrate reductase from Enterobacter
P C Moody1, N Shikotra, C E French
1Department of Biochemistry, University of Leicester, Adrian Building, University Road, Leicester LE1 7RH, England. pcem1@le.ac.uk
Acta Crystallographica. Section D, Biological Crystallography
|October 8, 1998
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 A. 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.