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With the discovery that RNA molecules could catalyze biological reactions came the realization that a single biopolymer could perform all of the functions required for life: coding and storage of genetic information, and biological catalysis. Even in the modern, protein-driven world, RNA molecules continue to perform a variety of cellular functions because, in the presence of magnesium ion, many RNAs can fold into stable three-dimensional structures that support biological functions, much like protein enzymes. We are studying two such RNA enzymes, group I introns and RNase P in order to understand how these molecules are able to fold and function. These molecules are 300-400 nucleotides in length and possess catalytic cores that are preformed in the absence of substrate, much like protein enzymes. Both catalyze cleavage of RNA phosphodiester backbones, yet they accomplish this by very different mechanisms. We are studying these enzymes using X-ray crystallography to determine the global fold of these RNA enzymes, how the nucleotide chain meanders in three-dimensional space. Additionally, we would like to see what functional groups of the RNA are in the active site and, using a combination of structural and biochemical experiments, learn how these contribute to catalysis. Finally, we would like to use biophysical methods to understand how these highly charged and functional group poor molecules are able to achieve structures that form specifically and fold cooperatively.