D. R. Davies

D. R. Davies is the published author name credited on a structural study of Tn5 transposase. The original 2000 paper lists a University of Wisconsin biochemistry affiliation. Its initials are retained here because the scientific byline establishes this contribution without establishing a full personal identity.^[ref]

Davies and collaborators determined a protein–DNA assembly at $2.3$ ångströms crystallographic resolution. The protein dimer held two DNA ends, with each end contacted by both subunits. The arrangement explained how one subunit could bind an end while the other supplied the active site for cleavage. It supplied a structural framework for understanding coordinated DNA transposition.^[ref]

The geometry is more revealing than a count of components. Imagine two subunits A and B and two DNA ends L and R. Knowing merely that the assembly contains two subunits and two ends leaves open an arrangement in which A independently processes L and B independently processes R. Contacts that span the two subunits instead couple recognition of an end to the partner's catalytic machinery. Such an arrangement provides a concrete reason why an isolated, correctly bound DNA end need not behave like the complete transpososome.

The quoted distance is $0.23$ nanometres, since one ångström is $0.1$ nanometres. Crystallographic resolution describes the spatial detail supported by the diffraction data; it is not a frame interval in a movie and does not mean that every atomic coordinate has an uncertainty of precisely $0.23$ nanometres. A static structure constrains possible reaction mechanisms, while the sequence and rates of chemical steps require additional evidence. The distinction matters whenever an attractive structural model is used to explain a dynamic enzyme reaction.