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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
Author(s) -
Rosário Ana Lúcia,
Sena Filipa V.,
Batista Ana P.,
Oliveira Tânia F.,
Athayde Diogo,
Pereira Manuela M.,
Brito José A.,
Archer Margarida
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15005178
Subject(s) - oxidoreductase , staphylococcus aureus , crystallization , pathogen , human pathogen , quinone , microbiology and biotechnology , x ray , chemistry , nad+ kinase , stereochemistry , biology , biochemistry , enzyme , bacteria , genetics , physics , optics , organic chemistry , gene
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 P 2 1 2 1 2 1 , 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.