Dame Louise Napier Johnson. 26 September 1940—25 September 2012

Abstract

Louise Johnson was a leading architect of protein crystallography and structural enzymology. She pioneered the application of the technique to understand how enzymes function at the molecular level. Much of our current knowledge of how enzymes catalyse chemical reactions with high specificity and how their activities are regulated, especially by cooperative allosteric transitions and reversible protein phosphorylation, has its origins in Louise's research on lysozyme, glycogen phosphorylase and protein kinases. Louise helped pioneer Laue protein crystallography as a method to elucidate dynamic structural changes in proteins. She was a strong advocate of synchrotron radiation as a tool for structural biology, working to establish third generation synchrotrons. Her delight in science and kindness toward her colleagues and students were an inspiration to those who knew her.