Crystallization and preliminary crystallographic characterization of the iron-regulated outer membrane lipoprotein FrpD fromNeisseria meningitidis

Abstract

Fe-regulated protein D (FrpD) is aNeisseria meningitidisouter membrane lipoprotein that may be involved in the anchoring of the secreted repeat in toxins (RTX) protein FrpC to the outer bacterial membrane. However, the function and biological roles of the FrpD and FrpC proteins remain unknown. Native and selenomethionine-substituted variants of recombinant FrpD43–271protein were crystallized using the sitting-drop vapour-diffusion method. Diffraction data were collected to a resolution of 2.25 Å for native FrpD43–271protein and to a resolution of 2.00 Å for selenomethionine-substituted FrpD43–271(SeMet FrpD43–271) protein. The crystals of native FrpD43–271protein belonged to the hexagonal space groupP62orP64, while the crystals of SeMet FrpD43–271protein belonged to the primitive orthorhombic space groupP212121.