Cloning, purification and preliminary X-ray crystallographic analysis of the OmpA-like domain of peptidoglycan-associated lipoprotein from Acinetobacter baumannii.

ABSTRACT: 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 P6(1) or P6(5), with unit-cell parameters a=b=72.58, c=44.65?Å, a calculated Matthews coefficient of 2.64?Å3?Da(-1) and one molecule per asymmetric unit.

SUBMITTER: Song JH 

PROVIDER: S-EPMC3515379 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature