Short range structural information from mass spectrometry and chemical crosslinking

Accurate short-range distance information of large protein complexes can be obtained by inserting chemical crosslinks between protein subunits and then using mass spectrometry to identify the exact location where these bonds are formed. Recently, we have applied this approach to study the interaction of the  and  subunits of the bacterial polymerase III. Structural restraints from targeted crosslinking experiments were bioinformatically combined with the known structures of the individual subunits to compute a faithful model of the bacterial replisome core complex with more than 200 kDa molecular weight. (With K. Ozawa and N.E. Dixon at UoW)