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Nominated by: Prof Juri Rappsilber, Technische Universität Berlin (Berlin, Germany)
“Francis joined my lab as a postdoc at a time of major optimization of the crosslinking mass spectrometry (MS) workflow. At the time, we were making fundamental developments to analyze multi-protein complexes using this technology. However, many parameters had not yet been tested. Francis quickly realized that the goal of whole cell analysis of Mycoplasma pneumoniae by crosslinking MS would improve the entire methodological workflow with a firm eye on an important biological application. He initiated and drove the development of multi-dimensional chromatographic separation of crosslinked peptides (published in Science 2020) and the implementation of statistical error handling of the identified crosslinks (accepted at Nature Communications). He also enthused others in the lab to invest in optimization of various steps of the workflow and organized a weekly Tuesday morning club for lab experience exchange and discussion of results and plans. In this way, he became a central pivot for the lab.
Outside of the lab, he has been invited to give talks at international conferences. Importantly for the field, he has sought to build connections across the field of structural proteomics. This effort has kickstarted a standardization drive in the field. To this end, he has been an organizer of the Symposium on Structural Proteomics and the Berlin Proteomics Forum and has been invited as a reviewer in his own right. He will soon be starting his own lab and I’m sure will become a key player in the field of structural proteomics.”
Describe the main highlights of your bioanalytical work.
I am a post-doc in the bioanalytics department at the Technical University Berlin. Over the course of my career, I have been interested in developing high-throughput mass spectrometry methods for studying the structural organisation of proteomes, particularly methods that can be applied to proteomes in situ. In my PhD, I developed co-fractionation mass spectrometry techniques to infer protein complexes in organisms that were not genetically tractable. During my postdoc, I have developed the technology of crosslinking mass spectrometry to discover the topology of protein complexes inside cells. Identifying crosslinked peptides is a large bioanalytical challenge against the huge ‘background’ of linear peptides. This has involved four years of optimising all aspects of the crosslinking MS pipeline including chromatographic enrichment, mass spectrometry acquisition strategies, statistical approaches, and data analysis. A particular highlight has been pioneering the study of bacterial cells where we discovered the architecture of an unexpected super-complex between the RNA polymerase and the ribosome [PMID: 32732422]. This mass spectrometry-based approach allows for the analysis of the structure and dynamics of protein complexes inside cells, and I am convinced it will become a major bioanalytical technique in the future.
[Video edit by Luke Maberly]
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