Abstract
In the quest to understand how single-stranded DNA-binding proteins function and evolve at a molecular level, determination of their high-resolution three-dimensional structure using methods such as X-ray crystallography is indispensable. Here we present a collection of methods used in crystallographic studies of the single-stranded DNA-binding protein from the bacteriophage Enc34, from designing expression constructs through to protein production, purification, and crystallization, to determination and analysis of the protein’s three-dimensional structure. The chapter aims to shed light on all the essential stages in a structural study of a single-stranded DNA-binding protein, with a spotlight on procedures specific to X-ray crystallography to aid those interested in venturing into structural biology.
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Cernooka, E., Rumnieks, J., Kazaks, A. (2021). Structural Characterization of a Single-Stranded DNA-Binding Protein: A Case Study of the ORF6 Protein from Bacteriophage Enc34. In: Oliveira, M.T. (eds) Single Stranded DNA Binding Proteins. Methods in Molecular Biology, vol 2281. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1290-3_23
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DOI: https://doi.org/10.1007/978-1-0716-1290-3_23
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