Our new parts are all versions of the same modular system, a fusion protein formed from a bacterial transmembrane domain and a zinc-finger domain, with linker domains between domains and a FLAG-tag for immunofluorescence staining. Each transmembrane/zinc-finger domain is independently interchangeable with other transmembrane/zinc-finger domains, though not interchangeable between each other (i.e. the transmembrane domain cannot be swapped for a zinc-finger domain and vice versa).

   Our new parts are all versions of the same modular system, a fusion protein formed from a bacterial transmembrane domain and a zinc-finger domain, with linker domains between domains and a FLAG-tag for immunofluorescence staining. Each transmembrane/zinc-finger domain is independently interchangeable with other transmembrane/zinc-finger domains, though not interchangeable between each other (i.e. the transmembrane domain cannot be swapped for a zinc-finger domain and vice versa).

     <br> The purpose of this fusion protein is to allow bacteria (specifically Escherichia coli) to bind specific short double stranded DNA sequences at their surface; using immobilised DNA the cell should remain bound in place, or this protein can be used for cell identification (barcoding).

     <br> The purpose of this fusion protein is to allow bacteria (specifically Escherichia coli) to bind specific short double stranded DNA sequences at their surface; using immobilised DNA the cell should remain bound in place, or this protein can be used for cell identification (barcoding).