PlumX Metrics
Embed PlumX Metrics

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

Acta Crystallographica Section F: Structural Biology and Crystallization Communications, ISSN: 1744-3091, Vol: 66, Issue: 9, Page: 1119-1123
2010
  • 5
    Citations
  • 0
    Usage
  • 8
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

Article Description

Fe-regulated protein D (FrpD) is a Neisseria meningitidis outer 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 FrpD43-271 protein were crystallized using the sitting-drop vapour-diffusion method. Diffraction data were collected to a resolution of 2.25 Å for native FrpD protein and to a resolution of 2.00 Å for selenomethionine-substituted FrpD (SeMet FrpD) protein. The crystals of native FrpD43-271 protein belonged to the hexagonal space group P6 or P6, while the crystals of SeMet FrpD protein belonged to the primitive orthorhombic space group P22 2. © 2010 International Union of Crystallography All rights reserved.

Bibliographic Details

Sviridova, Ekaterina; Bumba, Ladislav; Rezacova, Pavlina; Prochazkova, Katerina; Kavan, Daniel; Bezouska, Karel; Kuty, Michal; Sebo, Peter; Kuta Smatanova, Ivana

International Union of Crystallography (IUCr)

Biochemistry, Genetics and Molecular Biology; Physics and Astronomy

Provide Feedback

Have ideas for a new metric? Would you like to see something else here?Let us know