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| Paper: |
Crystallization of Extremophile Proteins for Study of Dynamics Using X-Ray Diffraction |
| Volume: |
540, Compendium of Undergraduate Research in Astronomy and Space Science |
| Page: |
70 |
| Authors: |
Carlin Lee, Tzanko Doukov, Francis E. Jenney Jr., and Stephen Cramer |
| DOI: |
10.26624/TXJS2803 |
| Abstract: |
Extremophiles are organisms that survive under extreme environmental conditions that would be lethal for most organisms, making them valuable models for understanding how proteins maintain their structure and function under physical stress (Rothschild & Mancinelli 2001; Cavicchioli 2002). Comparing a homologous protein from these organisms adapted to different environments helps explain the molecular mechanisms that determine protein stability and flexibility (Siddiqui & Cavicchioli 2006; Pinney et al. 2021). In this study, we focused on the crystallization of proteins from extremophilic microorganisms, including three rubredoxins and one superoxide reductase from different extremophiles as the first step toward high-resolution structural characterization by X-ray crystallography (Guss 2010). Protein crystallization conditions were optimized using the hanging-drop vapor diffusion method while varying precipitant composition, salt concentration, and buffer conditions (Ferré-D’Amaré 1999). Through systematic screening, crystals were obtained for rubredoxins from Limnobacter profundi (Lp), Clostridium psychrophilum (Cpsy), Marinitoga piezophila (Mp) and Superoxide reductase from Pyrococcus furiosus (PfSOR). Establishing reliable crystallization conditions for these proteins provides the foundation for future diffraction experiments and structural analyses aimed at examining temperature-dependent protein behavior. These structures will contribute to ongoing efforts to understand how extremophile proteins remain functional across a wide range of environmental conditions and has applications in human health, biotechnology, and the search for life beyond our planet (Cavicchioli 2002; Fiala & Stetter 1986). |
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