Open AccessCrystallization and preliminary crystallographic characterization of the iron‐regulated outer membrane lipoprotein FrpD from Neisseria meningitidis
Author(s) -
Sviridova Ekaterina,
Bumba Ladislav,
Rezacova Pavlina,
Prochazkova Katerina,
Kavan Daniel,
Bezouska Karel,
Kuty Michal,
Sebo Peter,
Kuta Smatanova Ivana
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911003215x
Subject(s) - neisseria meningitidis , crystallization , bacterial outer membrane , characterization (materials science) , crystallography , materials science , chemistry , bacteria , biology , nanotechnology , biochemistry , gene , genetics , escherichia coli , organic chemistry
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 FrpD 43–271 protein were crystallized using the sitting‐drop vapour‐diffusion method. Diffraction data were collected to a resolution of 2.25 Å for native FrpD 43–271 protein and to a resolution of 2.00 Å for selenomethionine‐substituted FrpD 43–271 (SeMet FrpD 43–271 ) protein. The crystals of native FrpD 43–271 protein belonged to the hexagonal space group P 6 2 or P 6 4 , while the crystals of SeMet FrpD 43–271 protein belonged to the primitive orthorhombic space group P 2 1 2 1 2 1 .