Jo J. Jones

TL;DR: This work provides new insights into the mechanism of topoisomerase action and a platform for structure-based drug design of a new class of antibacterial agents against a clinically proven, but conformationally flexible, enzyme class.

TL;DR: The crystal structure of human 2D6 helps to explain how Asp-301, Glu-216, and Phe-483 can act as substrate binding residues and suggests that the role of PHe-120 is to control the orientation of the aromatic ring found in most substrates with respect to the heme.

TL;DR: Bioassays of chemically synthesized SCB1, and of its purified stereoisomers, suggest thatSCB1 acts in a highly specific manner to elicit the production of both actinorhodin and undecylprodigiosin, the two pigmented antibiotics made by S. coelicolor.

TL;DR: The three-dimensional high-resolution structure of the RNaseP protein from Staphylococcus aureus is determined by nuclear magnetic resonance (NMR) spectroscopy in solution and it is revealed that this protein has an alphabeta-fold, similar to the ribonucleoprotein domain, and a conserved arginine-rich motif does not bind single-stranded RNA.

TL;DR: The improved protocol was shown to be suitable for process scale-up and intensification and applicable to the accumulation of an untagged heterologous protein, cytochrome c(2) from Neisseria gonorrhoeae, which requires both secretion and extensive post-translational modification.