On Monday 30th October at 11AM (GMT) Wolfgang Baumeister will deliver the 2023 John Kendrew Lecture, ‘Cryo-electron tomography or the power of seeing the whole picture’. Wolfgang’s lecture will be delivered in the LMB’s Max Perutz Lecture Theatre and will also be streamed over Zoom where anyone who is interested is welcome to join.
Professor Dr. Wolfgang Baumeister is a German molecular biophysicist and biologist. His research focuses on the development of new tools and methods for the structural characterisation of molecules and cells. His particular focus is in cryo-electron tomography for molecular and supramolecular structures, explored in their native environments.
Wolfgang was born in 1946 in Wesseling near Cologne. He studied Biology, Chemistry and Physics from the Universities of Münster and Bonn and later obtained his Ph.D. from the University of Düsseldorf in 1973. From 1981 to 1982 he completed his Heisenberg fellowship at the Cavendish Laboratory in Cambridge. In 1983 he joined the Max Plank Institute of Biochemistry in Munich as a group leader, became Director of the Institute in 1988 and since 2021 has been Director emeritus and Scientific Member.
Wolfgang’s research has been recognised with numerous awards including the Otto Warburg Medal in 1998, the Louis-Jeantet Prize for Medicine in 2003, the Harvey Prize in 2005, the Ernst Schering Prize in 2006, the Ernst Jung Gold Medal for Medicine in 2018 and the Alexander Hollaender Award in Biophysics in 2022.
Traditionally, structural biologists have approached cellular complexity in a reductionist manner by studying isolated and purified molecular components. This ‘divide and conquer’ approach has been highly successful, as evidenced by the impressive number of entries in the PDB.
However, awareness has grown in recent years that only rarely biological functions can be attributed to individual macromolecules. Most cellular functions arise from their acting in concert. Hence there is a need for methods developments enabling studies performed in situ, i.e. in unperturbed cellular environments. Sensu stricto the term ‘structural biology in situ’ should apply only to a scenario in which the cellular environment is preserved in its entirety. Cryo-electron tomography (Cryo-ET) has unique potential to study the supramolecular architecture or ‘molecular sociology’ of cells. It combines the power of three-dimensional imaging with the best structural preservation that is physically possible to achieve.
We have used cryo-electron tomography to study the 26S proteasome, the main machinery for protein degradation, in a number of cellular settings revealing its precise location, assembly and activity status as well as its interactions with other molecular players of the cellular protein quality control machinery. Another pathway for the disposal of waste is autophagy. Cryo-ET has allowed to visualize the biogenesis of autophagosomes in great detail.
John Kendrew was born in Oxford in 1919 and first came to Cambridge in 1936 as a student at Trinity College, earning a First Class Honours in Chemistry. During World War Two, John was recruited to the Air Ministry Research Establishment where he worked on early radar applications, before returning to Cambridge in 1946 to join Max Perutz at the MRC Unit for Research on the Molecular Structure of Biological Systems (now the MRC Laboratory of Molecular Biology). His research focused on protein structure and in 1958 he produced the first three-dimensional structure of a protein: myoglobin. This discovery helped Max to discover the structure of haemoglobin the following year and, in 1962, they were jointly awarded the Nobel Prize in Chemistry. In the 1960’s John jointly founded the European Molecular Biology Organisation (EMBO) and helped create the European Molecular Biological Laboratory (EMBL) where he was the inaugural Director. He also founded and was Editor in Chief of the Journal of Molecular Biology. From 1981-1987 he was President of St John’s College, Oxford. He died in Cambridge on 23rd August 1997.