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The BAM Complex pp 215–225Cite as

Identification of BamC on the Surface of E. coli

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 1329))

Abstract

In order to relate the structural architecture of the BAM complex to its function in outer membrane protein assembly, the arrangement of each component within the complex is vital. This chapter explores the structure and topology of BamC, using a range of biochemical techniques to probe the topology and surface exposure.

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Acknowledgements

We acknowledge support from the National Health and Medical Research Council (NHMRC) for research funding through a NHMRC Program Grant 606788 and the Australian Research Council FL130100038. (to T.L.). C.T.W. is an ARC Laureate Fellowship Postdoctoral Research Associate and T.L. is an ARC Australian Laureate Fellow.

Author information

Authors and Affiliations

  1. Department of Microbiology, Monash University, Building 77, 23 Innovation Walk, Clayton Campus, Melbourne, VIC, 3800, Australia

    Chaille T. Webb & Trevor Lithgow

Authors
  1. Chaille T. Webb
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  2. Trevor Lithgow
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Corresponding author

Correspondence to Chaille T. Webb .

Editor information

Editors and Affiliations

  1. National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Laboratory of Molecular Biology, , Bethesda, Maryland, USA

    Susan Buchanan

  2. Department of Biological Sciences,, Markey Center for Structural Biology, Purdue University, West Lafayette, Indiana, USA

    Nicholas Noinaj

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Webb, C.T., Lithgow, T. (2015). Identification of BamC on the Surface of E. coli . In: Buchanan, S., Noinaj, N. (eds) The BAM Complex. Methods in Molecular Biology, vol 1329. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2871-2_17

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  • DOI: https://doi.org/10.1007/978-1-4939-2871-2_17

  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-2870-5

  • Online ISBN: 978-1-4939-2871-2

  • eBook Packages: Springer Protocols

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