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Paper: Protein Crystallization for the Study of Temperature-Dependent Extremophile Rubredoxin Dynamics
Volume: 540, Compendium of Undergraduate Research in Astronomy and Space Science
Page: 51
Authors: Caroline Cole; Kat Drumright; Tzanko Doukov; Stephen P. Cramer
DOI: 10.26624/BHTJ9840
Abstract: Extremophiles, organisms that thrive in conditions once thought incompatible with life, expand our understanding of biochemistry and the limits of life in our universe. Found in improbable environments such as deep sea sediments, boiling hot springs, and freezing permafrost, extremophiles exhibit the remarkable adaptability of life’s biochemical structures that allows for survival under extreme temperature, pressure, pH, salinity, radiation, and combinations of such. By researching proteins in these extremophiles, the structure, function, and stability of Earth biomolecules in extreme environments can be further understood. In this study, we crystallize the rubredoxins of five different extremophilic organisms for the purpose of temperature-dependent structural analysis: Pyrococcus furiosus (Pf), hyperthermophilic; Polaromonas sp. EUR3 (P. sp. EUR3), psychrophilic; Polaromonas glacialis (Pg), psychrophilic; Thermotoga maritima (Tm), hyperthermophilic; Pyrococcus yayanosii (Py), hyperthermophilic piezophile. By comparing proteins from extremophiles with a variety of natural environments, an analysis of rubredoxin’s adaptability and stability across different temperatures can be studied if effective protein crystals are achieved. Each protein was crystallized using the hanging-drop method using a variety of conditions depending on rubredoxin and desired crystal morphology. Crystals were grown with the intent to be subjected to novel high-temperature x-ray diffraction, at temperatures as high as 383 K. The data taken from these rubredoxin crystals contributes to our understanding of the relation between molecular structure and function–informing biotechnological research and the search for extraterrestrial life.
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