Chemistry and Biochemistry
Physical and Mathematical Sciences
First Faculty Advisor
First Faculty Reader
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.
BYU ScholarsArchive Citation
Longhurst, Moriah, "Telsam-Target Protein Fusions Can Form Diffraction-Quality Crystals Without Direct Inter-Polymer Contacts" (2021). Undergraduate Honors Theses. 178.