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The Crystallographic Approach
Understanding enzyme function through X-ray crystallography

Our laboratory uses X-ray crystallography as a chief technique to study the structure and mechanism of metalloproteins. We focus on enzymes that contain complex metallocofactors and catalyze challenging chemical reactions, such as those that use radical-based chemistry or form organometallic bonds. We are interested in providing detailed three-dimensional information about the nature of complex metallocofactors to help understand how protein environment modulates reactivity. Using X-ray crystallography, we hope to gain insight into the function and mechanism of nature's complex protein machines.

Over the last few decades, advances in molecular biology, protein expression and purification, bioinformatics, computing power, and software development has made possible the structural determination of not just one enzyme, but several enzymes along an entire pathway. This has allowed us to better understand the interplay between enzymes in the production and manipulation of important metabolic molecules and natural products. Equally as important, these advances have also enabled us to solve mutiple structures of a single enzyme with bound substrates, analogs, and products, to acquire a series of "snapshots" of a single enzyme turnover. With these capabilities, X-ray crystallography has become a crucial element in studying enzyme mechanism.


From DNA to protein to crystal structure