What drew you to your research field?
When I was four years old I decided to follow in my mother’s footsteps and become a scientist. However, for a long time I was not sure whether I wanted to be a chemist or a physicist. I obtained an undergraduate degree in physics but specialized in biophysics in a department created by Professor David Shugar in Warsaw, Poland. Thus, in 1969 I applied to a graduate biophysics program at UCLA – but since that program was closed that year, my application was transferred to the newly established Molecular Biology Institute, where I became a graduate student of Professor David Eisenberg. And that is how I became a structural biologist.
What do you consider the most formative phase of your research career?
There were at least two different phases of my research career. Early on I was very much involved in the development of –, including the development of the first macromolecular crystallography beamline on a synchrotron, as well as a novel beamline for neutron diffraction. But as far as biologically targeted research is concerned, I think that my involvement in studies of HIV/AIDS that led to structural characterization of retroviral enzymes such as protease and integrase was the most important.
What do you see as the most important developments in your field in the past 10 years?
Without any doubt it was the development of cryoelectron microscopy (cryoEM) as the principal tool of structural biology. Crystallography was king from the 1950s until about 10 years ago, but now cryoEM is clearly the first choice. Crystallography will not go away but may never regain its status as the primary technique for investigating macromolecular structures.
Tell us about one of your favourite published paper from your lab
I would probably name the paper that did not originate primarily from my laboratory but was a result of a long collaboration with Professor Tom Blundell. That paper, published in 1991, described the unusual structure of nerve growth factor (NGF), an important small signalling protein (Nature 354, 411-414 (1991)). This publication was the final outcome of my fascination with NGF – I first learned about it when I briefly worked as a technician in the laboratory of Professor Rita Levi-Montalcini in Rome, back in 1969. I crystallized NGF in 1974, but it took another 17 years before its structure could be determined in Tom’s laboratory, with my limited participation.
What’s exciting in your research area right now?
I am no longer involved in experimental structural biology, but I found my niche in evaluating the incredibly important contents of the Protein Data Bank, with the aim of improving this database that is used by millions of scientists every year.
Two recent/key papers (not so recent, but I am proud of them):
Protein crystallography for aspiring crystallographers, or how to avoid pitfalls and traps in macromolecular structure determination. A. Wlodawer, W. Minor, Z. Dauter and M. Jaskolski, FEBS J., 280, 5705-5736 (2013). https://doi.org/10.1111/febs.12495
A brief history of macromolecular crystallography, illustrated by a family tree and its Nobel fruits. M. Jaskolski, Z. Dauter and A. Wlodawer, FEBS J., 281, 3985-4009 (2014). https://doi.org/10.1111/febs.12796
More information on the FEBS Open Bio plenary lecture at the 50th FEBS Congress
Alexander Wlodawer will deliver the FEBS Open Bio Lecture at the 50th FEBS Congress in Maastricht, the Netherlands on Monday 6th July 2026, on ‘Half century of structural biology through the eyes of one practitioner’.
Top photo by Daniel Boberg on Unsplash.