Abstract

Matti Saraste, (Figure 1) Program Coordinator for Structural and Computational Biology at the European Molecular Biology Laboratory (EMBL), died on May 21, 2001, in Heidelberg, Germany, at the age of 52. Matti Saraste was a pioneer of the combinatorial use of different structural biology methods, such as electron microscopy, X-ray crystallography, NMR spectroscopy, and computational techniques. Much of what is known today about the structural organization of large cytoskeletal proteins can be credited to Matti's research activities. Matti was esteemed for his pivotal contributions to the experimental and structural biology of transmembrane proteins and expertise in the field of bioenergetics. He was instrumental in promoting the integration of the structurally oriented research of signal transduction with the emerging opportunities from genetics, cell biology, and, more recently, proteomics and genomics. Prominent researchers at the EMBL, who have known and collaborated with Matti for many years, have expressed great shock and sorrow at his death. Matti was the driving force behind a better understanding of the mechanisms of vectorial tramsmembrane catalysis and protein-protein interactions in signaling pathways. They also remember him not only as an idealistic scientist who dreamed of a “better society,” but one who took substantial efforts to actualize and incorporate his personal ideals, at least within his own working environment. An advocate of philosophy and anthropology, Matti appreciated and was enriched by the diverse cultural backgrounds of his fellows and colleagues. Matti was a fellow for about one year at Moscow State State University, Moscow, Russia, between 1975 and 1976. He obtained his Ph.D. degree in biochemistry from the University of Helsinki, in Helsinki, Finland, in 1978. In the early 1980s, he spent two years as an EMBO-funded postdoctoral fellow in the laboratory of John E. Walker at the MRC Laboratory of Molecular Biology, in Cambridge, England, where he became centrally involved in setting up experiments on ATP synthases. He frequently described this time as a turning point in his career, during which he discovered the unique opportunities afforded by molecular structural biology. Part of his work provided the basis for the epochal X-ray structure solution of the F1 ATP synthase complex, which led to the Nobel prize being awarded to John Walker. Matti returned to Helsinki, where he became an independent researcher, and in 1989 was appointed Associate Professor of Biochemistry at the University of Helsinki. During these years, he developed double-tracked research interests. One scientific area was on respiratory systems, in particular, the integral membrane protein cytochrome oxidase; the second area was on large cytoskeletal proteins, where he focused on the heterotetrameric protein spectrin. Both systems have been of challenging complexity, not easily amenable to structural biology investigations. With the desire to make most efficient use of the state-of-the-art structural biology facilities available at that time and to experience the unique ambience of an international laboratory, he accepted the offer of independent group leader in the Structural Biology Program at the central laboratory of EMBL in 1990. With an initially small team of extremely motivated European graduate students and postdocs, he resumed his long-term projects: cytochrome oxidase and spectrin. During the subsequent years, he provided a series of pivotal contributions on various domains of these protein giants, often using cut/paste methods for tailoring these entities with the then-available molecular biology techniques. Thanks to the presence of some signaling domains like the Src homology 3 (SH3) domain and the pleckstrin homology (PH) domain in spectrin, he quickly became a scientific addict of signal transduction and rapidly developed a unique ability to put these domains into a wide context of biological processes. Based on his scientific achievements and his leading efforts for integration of the state-of-the-art molecular biology methods, he was appointed Coordinator of the Structural and Computation Biology Program at EMBL in 1996. Since then, he reshaped this program from a primarily methods-oriented one into a unit of mostly young, highly motivated and gifted group leaders with ambitious scientific goals in structural biology, integrated into the heterogeneous environment of the EMBL. Matti has also served as Editor of FEBS Letters since 1987, and more recently was appointed Managing Editor of the same journal. During his later days, he spent substantial effort in improving its peer review process, which led to a significant increase in its scientific impact. As much as Matti loved the international environment at the EMBL, he never lost his strong roots for Finland. Many previous graduate students and postdocs will never forget the unique ambience of social events in his home — where the specific Finnish ingredients, like fires made from juniper wood, smoked fish, and red-colored granberry spirits, served as obligatory additives. Matti liked nature, and being with him in natural habitats in the Alsace or the Black Forest was always a wonderful experience for his fellows. Being a humanitarian, Matti was also a stout supporter of the EMBL's new program “Science and Society.” Matti began his career as an antibourgeoisie-oriented student, reflecting the political climate 20 to 30 years ago; it was no surprise that he initially chose Moscow instead of some of the more prestigious universities in the United States to commence his international career. More recently, the EMBL afforded him a scientific environment that reflected some of his personal, life-long dreams. Scientists of the spirit of Matti are badly needed, especially during times when structural biology is experiencing another golden era, due to epochal determinations of giant protein complexes, while at the same time facing fundamental challenges by structural genomics approaches and a rapidly increasing commercialization of the available techniques. Matti Saraste will be deeply missed both by the scientific community and by his friends who loved him.

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