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Crystallization and preliminary X‐ray crystallographic analysis of PBPD2 from Listeria monocytogenes
Author(s) -
Cha Hyung Jin,
Jeong JaeHee,
Kim YeonGil
Publication year - 2014
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/s2053230x14005470
Subject(s) - listeria monocytogenes , orthorhombic crystal system , penicillin binding proteins , escherichia coli , crystallization , peptidoglycan , molecular replacement , crystallography , resolution (logic) , chemistry , bacteria , cell wall , microbiology and biotechnology , biochemistry , biology , crystal structure , gene , genetics , organic chemistry , artificial intelligence , computer science
Penicillin‐binding proteins (PBPs), which mediate the peptidoglycan biosynthetic pathway in the bacterial cell wall, have been intensively investigated as a target for the design of antibiotics. In this study, PBPD2, a low‐molecular‐weight PBP encoded by lmo2812 from Listeria monocytogenes , was overexpressed in Escherichia coli , purified and crystallized at 295 K using the sitting‐drop vapour‐diffusion method. The crystal belonged to the primitive orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 37.7, b = 74.7, c = 75.1 Å, and diffracted to 1.55 Å resolution. There was one molecule in the asymmetric unit. The preliminary structure was determined by the molecular‐replacement method.