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TssA from Aeromonas hydrophila: Expression, purification and crystallographic studies

Research output: Contribution to journalArticle

Samuel R. Dix, Ruyue Sun, Matthew J. Harris, Sarah L. Batters, Svetlana E. Sedelnikova, Patrick J. Baker, Mark S. Thomas, David W. Rice

Original languageEnglish
Pages (from-to)578-582
Number of pages5
JournalActa Crystallographica Section F: Structural Biology Communications
Issue number9
PublishedSep 2018

King's Authors


TssA is a core subunit of the type VI secretion system, which is a major player in interspecies competition in Gram-negative bacteria. Previous studies on enteroaggregative Escherichia coli TssA suggested that it is comprised of three putative domains: a conserved N-terminal domain, a middle domain and a ringforming C-terminal domain. X-ray studies of the latter two domains have identified their respective structures. Here, the results of the expression and purification of full-length and domain constructs of TssA from Aeromonas hydrophila are reported, resulting in diffraction-quality crystals for the middle domain (Nt2) and a construct including the middle and C-terminal domains (Nt2-CTD).

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