Biophysicist David Mervyn Blow played a pivotal role in the development of x-ray macromolecule crystallography. This discipline provides critical structural information for understanding the function of biological molecules and is particularly applicable in the field of drug design. David’s contributions to this outstandingly successful field have led to the detailed structure determinations of thousands of proteins. He died of lung cancer on 8 June 2004 in Devon, England.
David was born in Birmingham, England, on 7 June 1931. After completing his education at Kingswood School in Bath, he interrupted his studies to serve in the Royal Air Force as a glider pilot. He then pursued an undergraduate physics degree at Corpus Christi College of Cambridge University.
From there he continued research in 1954 under the direction of Max Perutz at the renowned Cavendish Laboratory, where he worked on the structural elucidation of the protein hemoglobin. Having a strong mathematical background, David was able to develop methods for analyzing the diffraction data collected from horse hemoglobin. That effort led to the successful elucidation of one of the first protein structures. (The structure of myoglobin was determined by John Kendrew at approximately the same time.)
David was fortunate to be part of the Perutz laboratory during a dynamic and exciting period in the field of structural and molecular biology. Also present in the lab at the time were James Watson and Francis Crick, who shared the Nobel Prize in Physiology or Medicine in 1962 with Maurice Wilkins. Another lab member was Kendrew; he and Perutz won the 1962 Nobel Prize for Chemistry. Being in the company of such great minds influenced David considerably; he pursued further exciting work toward protein structure determination. One of his most important contributions, and indeed a seminal paper in the field, was a joint work with Crick on the development of methods for minimizing errors that arise in the so-called isomorphous replacement technique.
David next came to the US, where he spent two years as a Fulbright scholar at the National Institutes of Health and MIT. During that period, he and Michael Rossmann worked closely to develop a method of molecular replacement, a technique for determining the three-dimensional structures of proteins based on expected structural similarities to other proteins for which structures are already known. They published a series of classic papers describing the theory and mathematics of the technique, which remains one of the most powerful methods for structure determination today. David returned to the Cavendish Laboratory in 1959. In 1962, the Cavendish Medical Research Council Unit for Work on Molecular Structure of Biological Systems, under the direction of Perutz, and another MRC-funded group led by Fred Sanger took residence in the newly established MRC Laboratory for Molecular Biology.
In close collaboration with Brian Hartley, also at the MRC Lab for Molecular Biology, David commenced structural studies of the digestive enzyme chymotrypsin. He recruited Brian Matthews and Paul Sigler to join him on that project. By 1967, they had successfully determined the structure of chymotrypsin, only the third protein to be structurally characterized. That work ultimately led to the elucidation of the catalytic mechanism (the specific atomic details of how catalysis occurs) for the large class of serine protease enzymes.
In 1977, David left Cambridge to take up a professorship in the biophysics section of the physics department at Imperial College London. He continued to work on structures of important proteins. It was during that time that I had the great fortune to pursue my doctoral work under David’s direction. He inspired his colleagues with the enormous passion he showed for his work. He was deeply committed to his students and strove not only to provide them with excellent training opportunities, but also to create an environment rich in learning and scientific interaction. Morning coffee and afternoon tea times with David in the “interaction room” provided opportunities for stimulating conversations on the nuances of data processing, data refinement and model building, and critical discussions on new structures from recent journal articles that littered the coffee table.
David played a key role in the formation of the British Crystallographic Association, of which he was president from 1984 to 1987. In 1991, he was persuaded to become the head of the physics department at Imperial College. However, due to ill health, he retired in 1994 and moved with his wife to North Devon, where he continued his scientific activities by giving lectures and writing papers. In 2002, his textbook entitled An Outline of Crystallography for Biologists (Oxford U. Press) was published and is an excellent work that is widely read by students.
Throughout his career, David received many honors, though he remained the extremely quiet and modest person known to so many of his friends and colleagues. He was elected fellow of the Royal Society in 1972, and received the British Biochemical Society’s CIBA Medal in 1967, the Charles Leopold Meyer Prize of the French National Academy of Sciences in 1979 (which he shared with David Phillips), and the Wolf Foundation’s Wolf Prize for Chemistry in 1987.
David’s spirit of scientific endeavor, inquiry, and enthusiasm and his warm and generous demeanor are missed by many.
