Barocas Lab Group |
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Paul Hattan
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Research The 3-D structure of a protein is extremely valuable information for life scientists, as it is the key to understanding the protein's behavior. Of the thousands of proteins in the human body, only a small fraction have known structures and behaviors. Currently, the only way to determine a protein's structure is via X-ray crystallography, which requires large, defect-free crystals, the cultivation of which is incredibly difficult. The Crystallization Micro-Array (CRYMA) is being designed to solve this problem. Consisting of protein, precipitant, and buffer solution reservoirs connected to several micro-reactors, the flow of each “ingredient” will be carefully controlled into each reactor to force optimal crystal nucleation and growth. In developing the CRYMA, several challenges are faced. Microchannels from each reservoir must cross to reach each of the reactors, requiring progress beyond the two-dimensional fabrication processes common MEMS and microfluidics. Once connected, flow regulation through the channels must be established with a combination of pumps and valves. Eventually, a crystal nucleation detection system will be developed, allowing independent, closed-loop crystallization control with little or no a priori knowledge of the protein or its phase behavior.
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