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.

Tools

Selected Publications

Hintze, B.J. and Johnson, S.J. (2010). ResDe: A New Tool for Visual Definition of Distance Restraints for Crystallographic Refinement. The Journal of Applied Crystallography 43, 1540-1542.

Jackson, R.N., Klauer, A.A., Hintze, B.J., Robinson, H., van Hoof, A. and S. J. Johnson, S.J. (2010). The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. The EMBO Journal. 29, 2205-2216.

Brandão, T.A.S., Hengge, A.C. and Johnson, S.J.  (2010) Insights into the reaction of protein tyrosine phosphatase 1B. Crystal structures for transition-state analogs of both catalytic steps. Journal of Biological Chemistry. 285(21), 15874-83.

Brandão, T.A.S., Robinson, H., Johnson, S.J. and Hengge, A.C. (2009). Impaired acid catalysis by mutation of a protein loop hinge residue in a YopH mutant revealed by crystal structures. Journal of the American Chemical Society. Journal of the American Chemical Society. 131(2), 778-786.

Johnson 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. Journal of Molecular Biology. 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.