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TssA from Aeromonas hydrophila : expression, purification and crystallographic studies

DOI: 10.1107/S2053230X18010439 DOI Help

Authors: Samuel R. Dix (University of Sheffield) , Ruyue Sun (University of Sheffield Medical School) , Matthew J. Harris (King's College London) , Sarah L. Batters (University of Sheffield Medical School) , Svetlana E. Sedelnikova (University of Sheffield) , Patrick J. Baker (University of Sheffield) , Mark S. Thomas (University of Sheffield Medical School) , David W. Rice (University of Sheffield)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 74 , PAGES 578 - 582

State: Published (Approved)
Published: September 2018

Open Access Open Access

Abstract: 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 ring-forming 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).

Journal Keywords: type VI secretion system; TssA subunit; Aeromonas hydrophila

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

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