Open AccessCloning, purification and preliminary X‐ray crystallographic analysis of the OmpA‐like domain of peptidoglycan‐associated lipoprotein from Acinetobacter baumannii
Author(s) -
Song Jung Hyun,
Lee Woo Cheol,
Park Jeong Soon,
Kim Seung Il,
Lee Je Chul,
Cheong Chaejoon,
Kim HyeYeon
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112038924
Subject(s) - peptidoglycan , acinetobacter baumannii , bacterial outer membrane , escherichia coli , microbiology and biotechnology , acinetobacter , chemistry , biology , bacteria , crystallography , cell wall , biochemistry , gene , genetics , antibiotics , pseudomonas aeruginosa
Peptidoglycan‐associated lipoprotein (Pal) is one component of the Tol–Pal system that is involved in maintaining the integrity and stability of the outer membrane. The C‐terminal OmpA‐like domain of Pal interacts noncovalently with peptidoglycan. In this study, the OmpA‐like domain of Pal from Acinetobacter baumannii was overexpressed in Escherichia coli strain BL21 (DE3), purified and crystallized using the vapour‐diffusion method. A native crystal diffracted to 1.4 Å resolution and belonged to space group P 6 1 or P 6 5 , with unit‐cell parameters a = b = 72.58, c = 44.65 Å, a calculated Matthews coefficient of 2.64 Å 3 Da −1 and one molecule per asymmetric unit.