Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal DUF490963-1138domain of TamB from Escherichia coli

Inokentijs Josts, Rhys Grinter, Sharon M. Kelly, Khedidja Mosbahi, Aleksander W. Roszak, Richard J. Cogdell, Brian O. Smith, Olwyn Byron, Daniel Walker

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4 Citations (Scopus)


TamB is a recently described inner membrane protein that, together with its partner protein TamA, is required for the efficient secretion of a subset of autotransporter proteins in Gram-negative bacteria. In this study, the C-terminal DUF490963-1138 domain of TamB was overexpressed in Escherichia coli K-12, purified and crystallized using the sitting-drop vapour-diffusion method. The crystals belonged to the primitive trigonal space group P3121, with unit-cell parameters a = b = 57.34, c = 220.74 Å, and diffracted to 2.1 Å resolution. Preliminary secondary-structure and X-ray diffraction analyses are reported. Two molecules are predicted to be present in the asymmetric unit. Experimental phasing using selenomethionine-labelled protein will be undertaken in the future.

Original languageEnglish
Pages (from-to)1272-1275
Number of pages4
JournalActa Crystallographica Section F: Structural Biology Communications
Publication statusPublished - 29 Aug 2014
Externally publishedYes


  • autotransporter
  • DUF490
  • Escherichia coli
  • TamB

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