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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

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

Song Jung Hyun JH Lee Woo Cheol WC Park Jeong Soon JS Kim Seung Il SI Lee Je Chul JC Cheong Chaejoon C Kim Hye-Yeon HY

Acta crystallographica. Section F, Structural biology and crystallization communications 20121030 Pt 11

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 t ...[more]

PMID: 23143247

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