An orthogonal purification strategy for isolating crosslinked domains of modular synthases.

ABSTRACT: Chemo-enzymatic methods for covalently crosslinking carrier proteins with partner enzymes within modular synthases hold promise for elucidating and engineering metabolic pathways. Our efforts to crystallize the ACP-KS complexes of fatty acid synthases have been complicated by difficulties in the purification of the crosslinked complex from the other proteins in the reaction. Here we present a solution that employs an orthogonal purification strategy to achieve the quantity and level of purity necessary for further studies of this complex.

SUBMITTER: Haushalter RW 

PROVIDER: S-EPMC3269958 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature