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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1351-3. doi: 10.1107/S1744309112038924. Epub 2012 Oct 30.

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

Author information

  • 1Division of Magnetic Resonance Research, Korea Basic Science Institute, 804-1 Yangcheong-ri, Ochang, Chungbuk 363-883, Republic of Korea.

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.

PMID:
23143247
[PubMed - indexed for MEDLINE]
PMCID:
PMC3515379
[Available on 2014/11/1]
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