Our work is centered on the structure and function of bacterial cell surface proteins involved in the capture, degradation and import of carbohydrates from the environment. A primary technique we use to understand how proteins interact with carbohydrates is protein crystallography, which allows us to visualize the protein-carbohydrate interface, and isothermal titration calorimetry, which we use to measure the affinity and specificity of the protein-carbohydrate interaction. We can then make predictions about how these proteins drive glycan uptake, and test these hypotheses in vivo by disrupting or mutating the genes encoding these proteins to determine how bacterial growth is affected. We also utilize single molecule fluorescence imaging (a collaborative effort with Julie Biteen in UM Chemistry) to track the movement of proteins during glycan uptake in order to visualize this metabolic process in real time. This interdisciplinary approach has allowed us to better understand the process of glycan uptake in key human gut symbionts including Bacteroides thetaiotaomicron, Bacteroides ovatus, Eubacterium rectale and Ruminococcus bromii