Our focus lies in understanding enzyme dynamics using a combination of biochemistry and biophysical tools. We are especially experienced in developing X-ray scattering techniques to understand the evolution of protein allostery, the choreography of biochemical pathways and enzyme catalysis, and correlated disorder in protein crystals.
In the Ando lab, we study the motions that proteins undergo during catalysis and regulation using a combination of biochemistry and biophysical tools. We focus on complex protein systems where we can apply our experience in technique development to propose novel solutions. We are especially interested in studying catalysis and regulation in metalloenzymes, proteins that use metal-containing cofactors to perform challenging - and often ancient - chemistry. As a structural enzymology lab, we are unique in that we often start with X-ray scattering, a structural technique that allows us to probe conformational disorder. For example, we use small-angle X-ray scattering (SAXS) to map the conformational landscapes of dynamic enzymes. By doing so, we not only gain intimate knowledge of the protein’s behavior in solution but also gain insight into experimental conditions that allow for hypothesis-driven structure determination by X-ray crystallography and cryo-electron microscopy (EM). Finally, we are challenging the notion that crystallography can only provide static snapshots. We are one of the few labs in the world harnessing information on correlated displacements contained in the diffuse scattering from protein crystals.