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Expression, purification, crystallization and preliminary X-ray diffraction analysis of a type II NADH:quinone oxidoreductase from the human pathogen Staphylococcus aureus.


ABSTRACT: 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 Staphylococcus aureus was recombinantly expressed in Escherichia coli, purified, crystallized and a crystallographic data set was collected at a wavelength of 0.873?Å. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 81.8, b = 86.0, c = 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.

SUBMITTER: Rosario AL 

PROVIDER: S-EPMC4388187 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray diffraction analysis of a type II NADH:quinone oxidoreductase from the human pathogen Staphylococcus aureus.

Rosário Ana Lúcia AL   Sena Filipa V FV   Batista Ana P AP   Oliveira Tânia F TF   Athayde Diogo D   Pereira Manuela M MM   Brito José A JA   Archer Margarida M  

Acta crystallographica. Section F, Structural biology communications 20150328 Pt 4


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 Staphylococcus aureus was recombinantly expressed in Escherichia coli, purified, crystallized and a crystallographic data set was collected at a wavelength of 0.873 Å. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 81.8, b = 86.0, c = 269  ...[more]

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