The structure of the DLH (C123S) with PMS bound indicates that the reason the enzyme is able to catalyse a wide range of dissimilar substrates is a consequence of its capacity to undergo a coordinated restructuring of the active site and associated regions of the molecule without compromising the stability of its tertiary fold.

A complex of the -subunit and the central domain of the γ-subunit from the ATP synthase of E. coli has been purified and crystallized and preliminary X-ray analysis has been carried out.