Degree Name



Chemistry and Biochemistry


Physical and Mathematical Sciences

Defense Date


Publication Date


First Faculty Advisor

James Moody

First Faculty Reader

Barry Willardson

Honors Coordinator

Wally Paxton


protein crystallography, crystallization chaperone, TELSAM, protein polymer, X-ray diffraction


X-ray diffraction is a robust method for determining the detailed 3D structures of specific proteins. However, this requires the formation of well-ordered protein crystals, a process that is time-consuming, expensive, and only has about a 10-30% success rate. New methods are needed to enable the efficient crystallization of challenging proteins. One such technique is explored here, which utilizes a protein polymer (the sterile alpha motif domain of the human protein translocation Ets leukemia, or TELSAM) as a crystallization chaperone to form a more ordered crystal lattice of target proteins and drive crystallization. This method was successfully used to crystallize, collect diffraction data, and solve the structure of a somewhat challenging target protein, the von Willebrand Domain of human capillary morphogenesis gene 2. This new structure provided additional information about how TELSAM functions as a crystallization chaperone and suggests interesting experiments to be carried out in future work.