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- W1963508729 abstract "Acinetobacter baumannii is a Gram-negative bacterium that is resistant to many currently available antibiotics. The protein LpxD is a component of the biosynthetic pathway for lipopolysaccharides in the outer membrane of this bacterium and is a potential target for new antibacterial agents. This paper describes the structure determination of apo forms of LpxD in space groups P21 and P4322. These crystals contained six and three copies of the protein molecule in the asymmetric unit and diffracted to 2.8 and 2.7 Å resolution, respectively. A comparison of the multiple protein copies in the asymmetric units of these crystals reveals a common protein conformation and a conformation in which the relative orientation between the two major domains in the protein is altered." @default.
- W1963508729 created "2016-06-24" @default.
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- W1963508729 date "2012-12-25" @default.
- W1963508729 modified "2023-10-17" @default.
- W1963508729 title "Structure determination of LpxD from the lipopolysaccharide-synthesis pathway of<i>Acinetobacter baumannii</i>" @default.
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- W1963508729 doi "https://doi.org/10.1107/s1744309112048890" @default.
- W1963508729 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3539694" @default.
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