The three dimensional structures of proteins or protein complexes can provide important clues concerning protein function and mechanism of action on a molecular level. The Rose laboratory is interested in using molecular biology coupled with X-ray crystallography and other biophysical techniques to study the structure function relationships of proteins, and their complexes with other proteins and nucleic acids. These studies are aimed at providing the structural basis of molecular action that can be exploited in the design of therapeutics and other applications. For example from our work on the Augmenter of Liver Regeneration (ALR), an interesting protein first isolated from regenerating rat liver, we were first to point out the novel ALR FAD binding motif and catalytic site.

Another project of the Rose group, in collaboration with Bi-Cheng Wang, is focused at improving the success rate of crystal structure determination from single wavelength anomalous scattering data. This project includes developing improved data collection methods, data collection using soft (wavelengths> 1.5) X-rays, and automating the synchrotron data collection and structure determination process.