Crystals : Clarity in Refraction
Creating drugs to target a particular protein or complex of proteins requires information about the molecule's basic structure. Protein crystallography is one of the earliest and most effective methods to ascertain this basic structure and contribute to the development of drugs. My research goal is to study the role of FoxM1 protein in cancer. FoxM1 has been observed as overexpressed in all types of cancer and has been shown to contribute in cancer's progression. Another protein Arf has been shown to bind to FoxM1 and relocate it to nucleolus where it is rendered inactive. Our lab has developed a small peptide fragment of Arf that binds to FoxM1 and relocates it to nucleolus just as the endogenous Arf protein, thus, negating the effect of overexpressed FoxM1. This could potentially lead to the development of a drug that targets FoxM1 without any adverse effects. One of the goals of my research is to crystallize the Arf-FoxM1 complex and find the structure of the co-crystal. To learn the skills necessary to accomplish my research goals, I took the Structures of Biopolymers course offered by the Biochemistry and Molecular Genetics department, where I had my first hands-on experience with protein crystallography as a part of an assignment. The image here shows multiple crystals of the protein lysozyme suspended in the drop where their nucleation started. Although the crystals are the same shape, they appear to be different in both shape and color when suspended in a different orientation. The different colors and shades result from the diffraction of a monochromatic light as it passes through the crystals suspended in multiple different orientations. Mastering the art of protein crystallography will greatly facilitate my research and, eventually, the development of a drug to target FoxM1.