Rate My Professor David Goldstone

David Goldstone's research specializes in structural biology, focusing on the structure and function of anti-retroviral host restriction factors. His academic interests include biochemistry, infectious disease, structural biology, drug design, and molecular evolution. He employs X-ray crystallography and related techniques to elucidate protein structures pertinent to pathogens such as Mycobacterium tuberculosis and retroviruses. Key publications from his body of work include 'Crystallization and preliminary diffraction studies of the C-terminal domain of the rpoB subunit of Mycobacterium tuberculosis RNA polymerase' (2005, Acta Crystallographica Section F), 'DsbC activation by the N-terminal domain of DsbD' (2001, Proceedings of the National Academy of Sciences), 'Structural Views along the Mycobacterium tuberculosis SecA2 Pathway' (2016, Structure), 'Elongation of the Poly-γ-glutamate Tail of F420 Requires Both Domains of the Mycobacterium tuberculosis Cofactor Biosynthetic Enzyme CofD' (2016, Journal of Biological Chemistry), and 'A method for analyzing the composition of viral capsid proteins by ICP-MS' (2019, Virology). These studies provide insights into molecular mechanisms of bacterial and viral processes, informing potential strategies for drug development and infectious disease intervention. As Head of School, he oversees teaching, research, and administrative functions, supporting postgraduate supervision in structural biology and related fields.