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Crystallization and preliminary diffraction studies of morphinone reductase, a flavoprotein involved in the degradation of morphine alkaloids
Author(s) -
Moody P. C. E.,
Shikotra N.,
French C. E.,
Bruce N. C.,
Scrutton N. S.
Publication year - 1997
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444997004046
Subject(s) - chemistry , flavoprotein , orthorhombic crystal system , crystallization , monomer , reductase , escherichia coli , pseudomonas putida , degradation (telecommunications) , enzyme , stereochemistry , biochemistry , crystallography , organic chemistry , gene , crystal structure , polymer , telecommunications , computer science
Morphinone reductase from Pseudomonas putida M10, a flavoprotein involved in the degradation of morphine alkaloids, was purified from an overexpressing strain of Escherichia coli and crystallized using the hanging‐drop vapour‐diffusion method. Diffraction data were collected to 2.5 Å. The I ‐centred orthorhombic cell has a monomer in the asymmetric unit. Preliminary molecular replacement calculations have been performed using Old Yellow Enzyme as the search model.

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