Open AccessPurification, crystallization and preliminary X‐ray crystallographic analysis of Lmo0540 from Listeria monocytogenes
Author(s) -
Jeong JaeHee,
Kim YeonGil
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110051754
Subject(s) - listeria monocytogenes , crystallization , penicillin binding proteins , crystallography , monoclinic crystal system , peptidoglycan , cell wall , virulence , chemistry , biosynthesis , resolution (logic) , microbiology and biotechnology , bacteria , penicillin , biochemistry , biology , crystal structure , enzyme , antibiotics , gene , genetics , organic chemistry , artificial intelligence , computer science
Penicillin‐binding proteins catalyze the biosynthesis of the peptidoglycan chains of the bacterial cell wall, which protects cells from osmotic pressure. Although Lmo0540 has been identified as a putative penicillin‐binding protein that contributes to the virulence of Listeria monocytogenes , the biochemical role of Lmo0540 remains unclear. To provide insights into its biochemical function, Lmo0540 was overexpressed, purified and crystallized by the sitting‐drop vapour‐diffusion method. Diffraction data were collected to 1.5 Å resolution using synchrotron radiation. The crystal belonged to the C ‐centred monoclinic space group C 2, with unit‐cell parameters a = 82.5, b = 75.7, c = 75.9 Å, α = γ = 90, β = 121.8°. A full structural determination is under way in order to elucidate the structure–function relationship of this protein.