BBB seminar: Edward Hough
Life at the atomic level. The role of protein crystallography in molecular biology
Institute of Chemistry and the National Center of Structural Biology (NORSTRUCT) at the University of Tromsø, Norway
Determination of the 3-dimensional structures of biological macromolecules using protein crystallography is rapidly evolving from being a research field in itself into a new role as a routine, though still demanding, technique in molecular biology.
A brief glimpse into the early days in Tromsø will lead into a presentation of our present work on the autosomal recessive lysosomal storage disease a-mannosidosis, which is due to a lack of lysosomal a-mannosidase activity.
If time permits, the lecture will conclude with a survey of current efforts and investments aimed at the automation of almost all of the methodology from target selection at the gene level to 3-D structure determination.
After his Ph.D. in protein crystallography at the Imperial College London in 1973 Dr. Hough continued his protein research activities at the University of Tromsø. He was a key person in establishing the first facility of protein crystallography in Norway and more recently also the newly created National Center of Structural Biology (NORSTRUCT) in Tromsø. During a period of 30 years he has been involved in determining the high-resolution crystal structure of a number of important proteins. Of particular biochemical interest are the pioneering structures of phospholipase C from Bacillus cereus (including its reaction products and a substrate analogue) and human phenylalanine hydroxylase (including its binary and ternary complexes), of benzamidine-inhibited trypsin, lysozyme, Rubisco, phospholipase D, chitotriosidase, the sulphonylurea receptor, alkaline phosphatase and most recently of lysosomal alpha-mannosidase. The relation between structure and function of the enzymes has been an important aspect in these studies. In addition, Dr. Hough has shown a great interest in protein engineering and evolution.