novel, biologically interesting and crystallization-feasible targets that were then designed into 96 different constructs. Processing of the 96 constructs was performed in parallel using simple automated applications of ligation-independent cloning, small-scale bacterial expression and purification, and solubility assessment. After processing the 96 constructs of 12 targets, I found that 16 constructs of three targets (25%) yielded soluble protein. From the three soluble targets, I have spent most time on two of these protein.The first protein is a CARD domain containing protein that interacts with Bcl10. The primary function of Bcl10 is to interact with CARD proteins through CARD-CARD interactions to regulate its activity [2]. The crystal structure of this CARD containing protein solved at 1.5 Å resolution revealed six anti-parallel α-helices, showing that this protein is indeed similar to other CARD proteins with known structures. Approaches to determine the interaction between these two CARD domain containing proteins are currently being applied.The second protein I worked on is a DUF59 domain containing protein with no function characterized yet. However, it has been reported that a family member is part of the MMXD protein complex involved in chromosome segregation [3]. I solved two crystal structures of this DUF59 domain protein to 1.8 Å resolution revealing, unusually, two different types of domain swapped-dimer. Functional characterization of this DUF59 domain containing protein, and of its domain swapping, is currently being investigated.
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