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The broad goal of our research is to understand biological function at a molecular level. Since biological activity is derived from the three-dimensional structure of a system, mechanistic details are often best described in the context of detailed structural information. The basic approach of the lab is to use x-ray crystallography techniques in combination with biochemical analysis to understand the structure and mechanism of proteins and macromolecular assemblies.
The lab has a strong interest in protein-nucleic acid interactions. Our current work focuses on themes central to replication and transcription. A particular emphasis is placed on proteins and complexes associated with regulation and coordination of replication and transcription processes. PIGS (Protein Information Gathering System)
Selected PublicationsJohnson SJ, Close D, Robinson H, Vallet-Gely I, Dove SL, Hill CP. (2008). Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa. J Mol Biol, 377, 1460-73. Johnson, S.J., Beese, L.S. (2004). Structures of mismatch replication errors observed in a DNA polymerase. Cell 116, 803-816. Johnson, S.J., Taylor, J.S., Beese, L.S. (2003). Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proc Natl Acad Sci USA, 100, 3895-3900. |