Domain-level rocking motion within a polymerase that translocates on single-stranded nucleic acid

An X-ray crystallographic structure is described for unliganded Vaccinia virus poly(A) polymerase monomer (VP55), showing the first domain-level structural isoforms among either VP55, it's processivity factor VP39, or the VP55-VP39 heterodimer. The occurrence of domain-level motion specifically in monomeric VP55 is consistent with the finding that the monomeric protein undergoes saltatory translocation whereas the heterodimer does not.

Improving the soluble expression of recombinant proteins by randomly shuffling 5' and 3' coding-sequence ends

Using basic technologies available in any laboratory, a method named `boundary shuffling' has been devised to generate orientated libraries for soluble domain selection.