Expression, purification, crystallization and preliminary X‐ray diffraction analysis of a type II NADH:quinone oxidoreductase from the human pathogen Staphylococcus aureus. Issue 4 (1st April 2015)

• Record Type: Journal Article
• Authors: Rosário, Ana Lúcia; Sena, Filipa V.; Batista, Ana P.; Oliveira, Tânia F.; Athayde, Diogo; Pereira, Manuela M.; Brito, José A.; Archer, Margarida
• Is Part Of: Acta crystallographica. Volume 71:Issue 4(2015:Apr.)
• Page Start: 477
• Page End: 482
• Publication Date: 2015-04-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X15005178
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>In recent years, type II NADH dehydrogenases (NDH‐IIs) have emerged as potential drug targets for a wide range of human disease causative agents. In this work, the NDH‐II enzyme from the Gram‐positive human pathogen <italic>Staphylococcus aureus</italic> was recombinantly expressed in <italic>Escherichia coli</italic>, purified, crystallized and a crystallographic data set was collected at a wavelength of 0.873 Å. The crystals belonged to the orthorhombic space group <italic>P</italic>2₁2₁2₁, with unit‐cell parameters <italic>a</italic> = 81.8, <italic>b</italic> = 86.0, <italic>c</italic> = 269.9 Å, contained four monomers per asymmetric unit and diffracted to a resolution of 3.32 Å. A molecular‐replacement solution was obtained and model building and refinement are currently under way.</p> </abstract>