معرفی
Professor Randy J Read FRS is a prominent structural biologist at the Cambridge Institute for Medical Research (CIMR), University of Cambridge, where he leads research in structural biology methods and applications. He holds a position in the Department of Haematology and maintains the Structural Medicine research group focused on protein structure determination through X-ray crystallography and cryo-electron microscopy. His work has significantly advanced computational methods for macromolecular structure determination.
Read's research interests span structural biology methodology development, particularly maximum likelihood approaches for protein crystallography. His group developed the Phaser software, which has become a standard tool in structural biology. His research also encompasses structural studies of medically-relevant proteins, including bacterial toxins like pertussis toxin and Shiga-like toxins, as well as serpins and other proteins involved in disease processes. His work bridges computational method development with biological applications, focusing on how protein structure informs function in disease contexts.
His recent publications demonstrate continued leadership in structural biology methodology, with significant contributions to integrating AlphaFold predictions with experimental approaches, likelihood-based methods for cryo-EM data analysis, and advanced molecular replacement techniques. The Phaser software continues to evolve as a critical tool for the structural biology community.
- Fellow of the Royal Society (FRS)
- Wellcome Trust Principal Research Fellow
- Extensive contributions to structural biology methodology
- Author of over 150 publications in top scientific journals
Read supervises research staff and students, with notable group members including Airlie McCoy and Alisia Fadini. His laboratory receives funding from the Wellcome Trust and the National Institutes of Health. His work has established him as a leading figure in the development of computational methods for protein structure determination, while maintaining strong connections to medically-relevant biological questions.
