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About

Rebecca Page is a structural biologist whose work bridges fundamental enzymology and practical protein production. Her primary research focuses on protein expression, crystallization, and structural determination, with a particular emphasis on developing cost-effective strategies for heterologous protein expression in *Escherichia coli*. Her most influential work, "Strategies to maximize heterologous protein expression in *Escherichia coli* with minimal cost" (2006), has garnered 227 citations, reflecting its lasting impact on laboratories worldwide seeking efficient protein production methods. Page has also made significant contributions to structural biology through her determination of the crystal structure of γ-glutamyl phosphate reductase (GPR) from *Thermotoga maritima*, an enzyme critical to proline biosynthesis. This work, published in 2003, provided atomic-level insights into the NADPH-dependent reduction mechanism of this important metabolic enzyme. Additionally, her 2008 paper on strategies for improving crystallization success rates addresses one of the most persistent bottlenecks in structural genomics—the challenge of producing diffraction-quality crystals. Through her research, Page has provided the scientific community with practical, implementable solutions for overcoming technical hurdles in protein structure determination, making her work essential reading for researchers in structural biology and protein engineering.