Degree Name

BS

Department

Chemistry and Biochemistry

College

Physical and Mathematical Sciences

Defense Date

2021-03-03

Publication Date

2021-03-19

First Faculty Advisor

James Moody

First Faculty Reader

Barry Willardson

Honors Coordinator

Wally Paxton

Keywords

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

Abstract

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.

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