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Can I read Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein on EtoBox?

Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein by Klaas M. Pos; Kay Diederichs is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein about?

Resistance of pathogens to antibiotics is often dependent on multi-drug export proteins that reside in the inner membrane of bacteria. This work describes the expression, purification, crystallization and preliminary crystallographic analysis of AcrB of Escherichia coli. Together with AcrA and TolC, AcrB forms a proton motive force dependent efflux pump of the resistance-nodulation-cell division (RND) transporter superfamily and is responsible for resistance towards many common antibiotics such as ciprofloxacin and novobiocin. AcrB crystallizes in space group R32, with unit-cell parameters a = b = 143, c = 513 A; the crystals diffract to 3.0 A resolution.

Who reads Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein?

It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.

Author
Klaas M. Pos; Kay Diederichs
Publisher
International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)
Published
2002
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)

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