Meet the Trainer – Pavel Baranov

Meet Pavel Baranov, Professor of Biomolecular Informatics at the University College Cork, Ireland. Pavel’s research group focuses on the understanding of how proteins are synthesised and how their synthesis is regulated.

Why did you choose to become a scientist?

When I was a toddler, I wanted to be a firefighter. Within a couple of years, I decided that being an astronaut would be more fun. A few more years passed, and I began to dream of becoming a scientist. I guess at that point I stopped growing and started living my dream.

What is your research focus?

My research group studies RNA translation. Translation is at the core of biology. Cells spend most of their energy on protein synthesis and the ribosome is the most abundant molecular machine in almost all cells. Ribosomal RNAs and tRNAs are the most conserved molecules across all kingdoms of life, and it is now apparent that proteins evolved earlier than DNA. Life as we know it relies on two main type of molecules not found outside of living systems – nucleic acids and proteins. It is the process of translation that connects these two chemistries together. I could hardly think of a more fundamental, interesting and challenging cellular process than translation.

Where do you see this field heading in the future?

As translation brings two chemistries together it is far more complex than other molecular process such as transcription and replication. Because of its complexity and the lack of tools to study it, studying translation is very challenging. The tools are now being developed, e.g. variations of ribosome profiling techniques, real-time single molecule imaging, cryo-EM microscopy, etc. The main change that I foresee is that translation will draw the attention of many more biomedical researchers, for better or worse.

What is your number one tip for people looking for scientific training?

Independent practice is the key in my opinion. After taking a course you may get the impression that you can do something, but it could be a false impression – you don’t really know if you can unless you have done it.

If you weren’t a scientist, what would you be?

Science is not a job for me, it is a dream. If I were not able to make my living as a researcher, I would have to find something else to make earnings, but I would not give up on my scientific interests.

You are organising the EMBO Practical Course ”Measuring Translational Dynamics by Ribosome Profiling” (3 – 9 May 2020). What is the greatest benefit of the course for the scientific community and what could the techniques in this course be used for in the bigger picture?

The invention of ribosome profiling is the most significant development in the field of protein synthesis since the deciphering of the ribosome 3D structure. Ribosomal profiling is a popular technique for measuring the rate of translation in addition to measuring RNA levels, but this was somewhat possible even before. The unique ability of ribosome profiling is the detection of which open reading frames are being translated in RNA. The application of ribosome profiling revealed that even in eukaryotes the same mRNA molecule is often used for making more than one polypeptide, and that our current knowledge of the human genome protein coding repertoire is still far from complete. In addition to detecting translated frames, ribosome profiling could be used to detect ribosome pauses.  We recently learned that such pauses could be used to regulate gene expression and other biological processes.  This course will provide trainees with everything what is needed for mastering this powerful technology, from hands-on experience in generating ribosome profiling data to bioinformatics analysis and the use of public data resources.

Interested in this course? Submit your application by 9 February!

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Best Poster Awards – The Non-Coding Genome

Taking place for the third time,  the EMBO|EMBL Symposium: The Non-Coding Genome (16 – 19 October 2019) brought together 305 RNA experts to discuss the roles of non-coding RNAs in both prokaryotes and eukaryotes, gene regulation and function. 

A total of 189 posters were presented, from which two were singled out as the winners by popular vote.

Characterization of the genomic and splicing features of long non-coding RNAs using bioinformatics approaches

Monah Abou Alezz is a Ph.D student in genetics, molecular and cellular biology at the University of Pavia, Italy. PHOTO: Monah Abou Alezz

Authors: Monah Abou Alezz, Ludovica Celli, Giulia Belotti, Silvia Bione, Institute of Molecular Genetics L. L Cavalli-Sforza – National Research Council, Italy

Recent developments in deep sequencing approaches have simulated the continuous discovery of a significantly large number of novel long non-coding RNA (lncRNA) genes loci in the genomes. Long non-coding RNAs are recognized as a new class of regulatory molecules despite very little is known about their functions in the cellular processes. Due to their overall low expression level and tissue-specificity, the identification and annotation of lncRNA genes still remains challenging. The characterization of lncRNAs’ features is crucial to understand and get functional insights on their mechanisms of action. We exploited recent annotations by the GENCODE compendium to characterize the genomic and splicing features of long non-coding genes, in comparison to protein-coding ones, in the human and mouse genome by using bioinformatics approaches. Our analysis highlighted differences between the two classes of genes in terms of gene architecture regarding exons and introns length, GC-content, and the combinatorial patterns of chromatin marks and states. Moreover, significant differences in the splice sites usage were observed between long non-coding and protein-coding genes. While the frequency of non-canonical GC-AG splice junctions represents about 0.8% of total splice sites in protein-coding genes, we identified a remarkable enrichment of the GC-AG splice sites in long non-coding genes, both in human (3.0%) and mouse (1.9%). In addition, we identified peculiar characteristics of the GC-AG introns in terms of donor and acceptor splice sites strength, poly-pyrimidine tract, intron length, and a positional bias of GC-AG junctions being enriched in the first intron. Genes containing at least one GC-AG intron were found conserved in many species across large evolutionary distances, more prone to alternative splicing and a functional analysis pointed toward their enrichment in specific biological processes such as
DNA repair.

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MirGeneDB 2.0: The metazoan microRNA complement

Bastian Fromm is a Senior Researcher at Science for Life Laboratory, Stockholm University, Sweden. PHOTO: Bastian Fromm

Authors: Bastian Fromm (1), Diana Domanska (2), Eirik Hoye (3), Vladimir Ovchinnikov (4), Wenjing Kang (5), Ernesto Aparicio-Puerta (6), Morten Johansen (7), Kjersti Flatmark (3), Anthony Mathelier (8), Hovig
Eivind (3), Michael Hackenberg (6), Marc Friedländer (5), Kevin Peterson (9)

Non-coding RNAs (ncRNA) have gained substantial attention due to their roles in human disorders and animal development. microRNAs (miRNAs) are unique within this class as they are the only ncRNAs with individual gene sequences conserved across the animal kingdom. Bona fide miRNAs can be clearly distinguished from the myriad small RNAs generated in cells by a set of unique criteria. Unfortunately, recognition and utilization of these clear and mechanistically well understood features is not a  common practice. We addressed this by extensively expanding our curated miRNA gene database MirGeneDB to 45 organisms that represent the breadth of Metazoa. By consistently annotating and naming more than 11,000 miRNA genes in these organisms, we show that previous miRNA annotations contained not only many false positives, but surprisingly many false negatives as well. Indeed, curated miRNA complements of closely related organisms are very similar and can be used to reconstruct evolution of miRNA genes, families and biogenesis across more than 1 billion years of evolution. MirGeneDB represents a robust platform for providing deeper and more significant insights into the biology of miRNAs, possible sources of mis-regulation, and evolutionary mechanisms. MirGeneDB is publicly and freely available under http://mirgenedb.org/.

View PDF Poster

Fromm, B. et al. MirGeneDB 2.0: the metazoan microRNA complement. Nucleic Acids Research, gkz885, (2019), https://doi.org/10.1093/nar/gkz885

(1) Science for Life Laboratory, Sweden
(2) Department of Informatics, University of Oslo, Oslo, Norway
(3) Department of Tumor Biology, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, Oslo, Norway
(4) School of Life Sciences, Faculty of Health and Life Sciences, University of Nottingham, United Kingdom
(5) Stockholm University, SciLifeLab, Sweden
(6) Department of Genetics, Faculty of Sciences, University of Granada, Granada, Spain
(7) Institute for Medical Informatics, The Norwegian Radium Hospital, Oslo University Hospital, Oslo, Norway
(8) Centre for Molecular Medicine Norway (NCMM), Nordic EMBL Partnership, University of Oslo, Oslo, Norway
(9) Department of Biological Sciences, Dartmouth College, Hanover, New Hampshire, United States of America


Working on your own conference poster? Then check out 10 tips to create a scientific poster people want to stop by .

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Best Poster Awards – EMBO Workshop: Tools for Structural Biology of Membrane Proteins

183 researchers convened at the Centre for Structural Systems Biology (CSSB) in Hamburg, Germany, for the recent EMBO Workshop: Tools for Structural Biology of Membrane Proteins (7 – 9 October 2019) to present and discuss new technologies and approaches applied in studying membrane protein structure, dynamics and functions.

Out of the 82 posters presented, 6 were awarded a poster prize based on popular vote. Here we present the poster abstracts of four of the winners.

Structural insights into the role of the conserved ATPase component, EccC, in the mycobacterial T7SS

Katherine Beckham is a postdoctoral fellow in Matthias Wilmanns’ group at EMBL Hamburg. PHOTO: Katherine Beckham

Authors: Katherine Beckham (1), Luciano Ciccarelli (1), Mandy Rettel (2), Mikhail Savitski (2), Jan Kosinski (1), Annabel
Parret (1), Matthias Wilmanns (1)

Mycobacteria have a unique membrane structure with a complex hydrophobic outer-membrane rich in mycolic acids. To transport substances across this impermeable barrier, mycobacteria rely on a highly specialised translocation machinery – the Type VII secretion system (T7SS). Pathogenic mycobacteria encode up to five distinct T7SSs ESX-1 to 5 [1]. Our previous work characterised the structure of the of the inner-membrane complex of the ESX-5 T7SS from Mycobacterium xenopi using negative stain electron microscopy, revealing a hexameric 1.8 MDa complex comprising the four conserved core components: EccB5, EccC5, EccD5 and EccE5 [2]. The large cytosolic domain of EccC5, an FtsK/SpoE-like ATPase, is absent in our current EM map due to its conformational flexibility, which may be required to accommodate a range of protein substrates. Our current work aims to understand the role of EccC5 in secretion. In isolation this component can oligomerise into a hexameric ring-like conformation, as observed for other ATPases in this family. In addition, chemical cross-linking of the ESX-5 complex coupled with mass spectrometry (XL-MS) supports the oligomerisation of EccC5 in the secretion complex, suggesting that it may form a channel or ‘translocation tunnel’. Thus, we propose that EccC5 may exist in two conformational states: an extended, flexible monomeric state and a more compact hexameric state. Using an integrative structural biology approach, we are combining structures of isolated proteins derived from X-ray crystallography and electron microscopy studies with XL-MS data. Together these data aim to further elucidate the secretion pathway across the mycobacterial cell envelope.

References:
[1] Houben, E. N. G., et al. Take five — Type VII secretion systems of Mycobacteria. Biochim. Biophys. Acta – Mol. Cell Res.1843, 1707–1716 (2014).
[2] Beckham, K. S. H. et al. Structure of the mycobacterial ESX-5 type VII secretion system membrane complex by single-particle analysis. Nat. Microbiol.2, 17047 (2017).

(1) EMBL Hamburg, Germany, (2) EMBL Heidelberg, Germany

Poster currently not available


Dissection of protonation sites for antibacterial recognition and transport in QacA, a multidrug efflux transporter

Puja Majumder is a Ph.D student at the Indian Institute of Science. PHOTO: Puja Majumder

Authors: Puja Majumder (1), Shashank Khare (1), Arunabh Athreya (1), Nazia Hussain (1), Ashutosh Gulati (2), Aravind Penmatsa (1)

Emergence of multidrug-resistance poses serious threat to the society. One of the effective way by which bacteria gain drug resistance is through active efflux of antibiotics and other antibacterial compounds using multidrug efflux transporters. Among the battery of efflux pumps present in pathogenic bacteria, our work is focused on QacA, a drug-proton anitiporter (DHA) with 14-transmembrane helices that provide resistance to methicillin resistant Staphylococcus aureus (MRSA) strain, with homologs present in other pathogenic organisms. QacA is a highly promiscuous transporter, capable of effluxing diverse array of monovalent and divalent cationic antibacterial compounds and dyes. This study using a homology model, dissects the role of six protonatable residues present in the transport vestibule of QacA. Systematic mutagenesis resulted in identification of D34 (TM1) and E407 (TM13) as crucial residues and D323 (TM10) and D411 (TM13) as conditional residues needed for transport process of QacA. Whole cells, inside-out vesicles, substrate-induced proton release and microscale thermophoresis based assays were used to investigate the transport and binding properties of the transporter and its mutants. The activity of purified protein was checked with reconstituted QacA in a proteoliposome using substrate-induced proton transport assay. We identify two sites, D34 and D411 playing vital role in recognition of most of the substrates tested while E407 facilitates substrate efflux as a protonation site. It was also observed that E407 has an additional role as a recognition site for the transport of dequalinium, a divalent quaternary ammonium compound. These observations rationalize the promiscuity at the residue level of QacA for diverse substrates. The study identifies the role of acidic residues in QacA with implications for substrate recognition, promiscuity and processive transport in multidrug efflux transporters, related to QacA.

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(1) Indian Institute of Science, India, (2) Stockholm University, Sweden


Biophysical analysis of circularized MSP nanodiscs for structural studies

Melina Daniilidis is a Ph.D student in Prof. Dr. Franz Hagn’s group at the Bavarian NMR Center (BNMRZ) of the Technical University of Munich. PHOTO: Melina Daniilidis

Authors: Melina Daniilidis (1), Ralf Stehle (1), Franz Hagn (1,2)

Structure and dynamics of membrane proteins are crucial aspects for understanding functional properties of this protein class. Unfortunately, stabilizing them in their isolated form is still difficult. By incorporating membrane proteins into nanodiscs, they can be studied in a native-like
environment using biochemical and structural methods. However, thermal and long-term stability of small nanodiscs limit these studies and make it difficult to carry out nuclear magnetic resonance spectroscopy (NMR) measurements at elevated temperatures. Circularized membrane scaffold proteins (MSPs) produced via split-inteins have been shown to be more stable and homogenous than their linear counterparts. However, their biophysical properties, as well as suitability for membrane protein insertion and structural studies have not yet been assessed in a systematic manner. Thus, we examined circular and linear nanodiscs of varying size using several biophysical methods. An important issue for NMR structural studies is that the size and shape of circular nanodiscs do not expand above the phase transition temperature, increasing their homogeneity and reducing their size as compared to linear nanodiscs at high temperatures. 1H,15N-TROSY experiments could demonstrate that circular MSP1D1 nanodiscs with incorporated VDAC-1 are stable at higher temperatures, making it possible to obtain high-resolution NMR spectra of superior quality. Furthermore, NMR relaxation experiments were carried out to compare rotational correlation times of VDAC-1 in circular and linear nanodiscs, respectively. Despite the higher molecular weight, the circular nanodiscs showed lower rotational correlation times, which corroborated the biophysical results on the temperature-dependecy of the nanodisc diameter and homogeneity. The presented data demonstrate that these very stable circularized MSPs are well applicable to the study of membrane proteins in a lipid environment by NMR, but also other structural methods like electron microscopy.

(1) Technical University of Munich, Germany, (2) Helmholtz Zentrum München, Germany

Poster currently not available


Reconstitution of the activity of RND efflux pumps into proteoliposomes

Dhenesh Puvanendran is a Ph.D student at the Institute of Physical and Chemical Biology in Paris, France. PHOTO: Dhenesh Puvanendran

Authors: Dhenesh Puvanendran, Quentin Cece, Martin Picard, IBPC, France

Efflux pumps are the major systems in bacterial resistance against antibiotics. They are classified by the energy needed to be active (ATP hydrolysis or ion counter-transport). Efflux pumps from the RND (Resistance, Nodulation, and cell Division) family use a proton gradient to be active and are composed of three proteins: a membrane fusion protein (MFP) and a transporter (RND) in the inner membrane, and an Outer Membrane Factor (OMF) localized in the outer membrane. We focus on the MexA-MexB-OprM efflux pump from Pseudomonas aeruginosa.The overall goal of my research is to measure in vitro the velocity of transport by efflux pumps. To that end, we reconstitute MexA and MexB as one population of proteoliposome, and OprM as another population of proteoliposome. The whole tripartite pump forms upon association of the respective populations of liposomes. The proof of concept of this method has already been described, leading to a qualitative monitoring of transport. We now work at defining a reconstitution procedure amenable to now quantify the rate of transport. To do so we take extreme care to precisely determine the efficiency of protein reconstitution and the type of lipids component used to perform liposomes. I will present the roadmap towards the rational, step-by-step, reconstitution of the MexA-MexB-OprM efflux pump as well as the methodologies that are undertaken to measure the velocity of transport, and possible perspectives regarding the screening of efflux pump inhibitors.

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The other award-winning posters are:

Novel antigen-binding chimeric proteins as tolls in crystallography and cryo-EM of membrane proteins presented by Thomasz Uchanski, Vrije Universiteit Brussel, Belgium

Cryo-Electron tomography of synaptic vesicle fusion junctions presented by Lucy Ginger, MRC Laboratory of Molecular Biology, United Kingdom


Working on your own conference poster? Then check out 10 tips to create a scientific poster people want to stop by .

 

 

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Meet the Trainers – Raffaele Calogero, Jeroen Krijgsveld, Lennart Martens

This month we have not one but three trainers we would like to introduce you to. Meet Raffaele Calogero, Jeroen Krijgsveld and Lennart Martens, organisers and trainers at the EMBL Course: Analysis and Integration of Transcriptome and Proteome Data (2 – 7 February 2020).

What is your research focus and why did you choose to become a scientist?

RC: I have a background in molecular biology, but since 1999 I have been working in transcriptomics data analysis and tool development. I became a scientist because I loved the idea of investigating new unknown topics every day.

LM: My research focus is bioinformatics, which stems directly from becoming completely taken in by computers at an early age. Like many of my generation, I started out with a Commodore 64 when I was 8, and had written my first (very, very simple :)) program in BASIC after two weeks. But my link with science came about after I stumbled across an episode of Jacob Bronowski’s ‘The Ascent of Man’ a few years later (I think I was 10 or 11) on Saturday morning on television, and this inspired a lifelong interest in anything scientific. All in all, I consider myself extremely lucky to be able to combine my passion for computers with my passion for science, and make a living out of it!

JK: My research focus is on proteomics, where we develop and apply mass spectrometry-based technologies to understand the intricate machineries used by cells to respond to their environment. Curiosity to understand how things work is as an important motivation for our current research as it was for me during my studies. Becoming a scientist has always felt a natural path for me to follow, and I have never seriously considered doing anything else. Although at the same time, when looking back, I realise how fortunate I have been being given the opportunity to follow my interest and move between fields. This is due in no small part to having training opportunities and stimulating environments at the various stages of my career!

Where do you see this field heading in the future?

RC: Data integration is the new upcoming frontier for biological studies, and transcriptomics and proteomics are going to be important players in the game.

JK: Proteomics has come a long way in the last 2 decades, reaching its current ability to characterise thousands of proteins in a single experiment, and do this across multiple experiments. I expect that during the next 5-10 years we will see how these investments will pay off, helping to understand processes at the protein level very similar to the way this has been achieved in genomics. After transitioning from a technology exclusively for physicists to a useful tool used by biologists, the next big step to be made is to implement mass spectrometry in the clinical arena. Integration with genomic methods and data types will be key to drive this forward.

LM: Bioinformatics is slowly taking over much of large-scale biology. Of course, focused biochemical and molecular biology research will remain the staple of the life sciences, but our ability to process and interrogate very large amounts of (potentially even heterogeneous) data is transforming our ability to generate new leads, new ideas, and to shed a much more holistic view on life at the molecular level. And with the advent of extremely powerful parallel computing, the field of machine learning has received an enormous boost, further increasing our ability to spot previously hidden patterns in our data. So it’s an exciting time in bioinformatics, with lots of new areas of research opening up to us for the first time! We’re going to continue having a lot of fun for a long time!

How has training influenced your career?

JK: This has been fundamental, in different ways. One is in a formal way, where classes and courses have been key to shaping a foundation, and helping to fill specific knowledge gaps. The second is less formal, which to me has been at least equally important, where I got trained by working in different research environments together with people of different backgrounds.

RC: In my role as an associate professor, training is part of my everyday life. I am involved in many advanced courses through my university, both in Europe and in Asia, and I think that courses are useful for both participants and instructors. The former grab the knowledge from the latter and the latter get new fresh view points from the former.

LM: Many of the excellent teachers I have studied with have left a deep impression on me, and guided my career path indirectly. As to providing training, it is one of the aspects of my job that I most cherish. For me, the importance of sharing and spreading knowledge resonates very closely to the core principles of science: by sharing and exchanging knowledge, all participants in the teaching experience gain something. In all, the biggest contribution that training has had to my career, is in greatly enhancing my ability to be creative in a productive way.

What is your number one tip for people looking for scientific training?

LM: Go for it, and seek out courses taught by those rare experts that both intimately know their field, but can also clearly communicate about the essence of that field. You don’t want to only grasp the current ‘hot’ method at a user level, but rather want to understand how that field works, how it has evolved, and how the current methods fit in with this. Courses that focus on these aspects deliver knowledge that lasts for much longer!

JK: It is two-fold: find a course that gives you the theoretical foundation of an area or topic you would like to venture into. After this, I think it is essential to ‘internalise’ this knowledge, so I would advise you to find a collaborator or colleague to help you along the path to use the acquired knowledge. It is like driving a car: you need to get a driver’s license to be allowed on the road, but you really learn how to do it by practicing afterwards.

If you weren’t a scientist, what would you be?

RC: Definitively a Medical Doctor.

LM: Most likely a software developer or systems architect of some sort. I worked in industry for a few years after my Masters degree, and then chose to pursue a PhD rather than take a very nice position at Microsoft. So if I had made a different choice then, I’d probably still be in IT!

JK: I have never really been in a situation where I had to choose between being a scientist or do something else, but thinking about it now I would like to think I would be a writer, a novelist. The reason is that I like writing, and it is part of my every day job, however writing papers and proposals comes with a lot of constraints and requirements. Making up stories without the boundaries of page limits, allowing fantasy and imagination, in an expanded vocabulary and, above all, in my mother tongue sounds all very appealing to me. Maybe one day. 🙂

You are organising the EMBL Course: Analysis and Integration of Transcriptome and Proteome Data (2 – 7 February 2020). What is the greatest benefit of the course for the scientific community and what could the techniques in this course be used for in the bigger picture?

JK: The greatest benefit is that it allows participants to have a look ‘over the fence’: most participants usually have a background either in genomics or proteomics, and being exposed to both aspects – along with the technologies and methods used in these fields – allows them to ask questions they may not have thought about before. What we try to achieve is that they could even go a step further, and integrate the new knowledge in their research to gain a more complete picture of the biological systems they are using.

LM: The course is unique in that it brings together the two key fields of research to understand cellular functional: transcriptomics, which traces the usage of the information in the genome in a given cell, and proteomics, which shows the actual biochemical and signalling capability of a given cell. There is important information at each of these levels, and these are moreover more complementary than many might think.

Of course, gene regulation provides important insights into a cell’s internal processes, but proteins are not only made or broken down, they are also closely regulated at the protein level. A complete picture of a cellular process thus requires insight into (and thus data from) both the gene expression level as well as the protein level. This is where this course provides the right skills for researchers; teaching them how to integrate data from their transcriptomics and proteomics experiments.

The usefulness for the bigger picture is therefore more or less implicit: by combining transcriptomics and proteomics, a much more complete picture of cellular functioning can be obtained. And let’s be honest, isn’t that what all of us really want to obtain, after all? 🙂

RC: I think the phrase of Claudia Manzoni in the abstract of her paper in Briefing in Bioinformatics in 2016 (Volume 19, Issue 2, March 2018, Pages 286–302) “Our work intends to target students and researchers seeking knowledge outside of their field of expertise and fosters a leap from the reductionist to the global-integrative analytical approach in research” is a perfect explanation for our course.


Interested in this course? Apply by 10 November!

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Cooking for EMBL Events

Head of the EMBL Canteen and Cafeteria Michael Hansen (front, in grey) with his dedicated team. PHOTO: Marietta Schupp/EMBL

Anyone who has ever set foot in the EMBL Canteen is sure to go away wanting more. It’s no coincidence that the canteen has a reputation for serving some of the best food in the Heidelberg area.

So what is their secret?

Head chef Michael Hansen’s team of 29 (23 people in the canteen and 6 in the cafeteria) work tirelessly to cater for over 800 members of staff daily and over 6000 conference and course participants annually. Besides the great dedication of his staff – which involves regular evening and weekend shifts – he places great emphasis on the quality and freshness of the groceries they use.

“We buy our meat, fruit, vegetables, bread and eggs from local suppliers. For us it is important that the groceries have the shortest route so that they are as fresh as possible when they get to us. Our furthest supplier is 90 km away. For food that is not produced in Germany, such as olive oil, we do have to order from abroad, but we do that directly with the producers without going through a distributor.”

Everything is then freshly prepared and cooked before it is served, with close attention paid to nutritional value. This is especially important for the EMBL kindergarten, which caters for over 100 children of staff.

In 2018, the EMBL Canteen cooked for 6430 course and conference participants, and for this purpose used:

  • 32 crates of salad
  • 160 kg onions/garlic (imagine how many tears must have been shed!)
  • 225 kg fish
  • 225 kg potatoes
  • 290 kg meat
  • 803 kg fruit
  • 935 kg vegan/vegetarian dishes
  • 1,607 kg vegetables
  • 1,376,020 l coffee was served

“In the EMBL spirit, the canteen team is truly international, employing people from 12 nations who, despite their differences, have one thing in common – their love for cooking!  One of the reasons I became a cook is because of food’s power to unite people. And here I see this every day. Preparing one meal requires real team work. Everybody gets together and takes one step of the process so that all is done in the most efficient way, but still has great taste.”

Here is one of the canteen’s most popular recipes, named after Thomas Graf, EMBL Alumnus (1983 – 1998) and currently Senior Scientist at the Centre for Genomics Regulation in Barcelona, Spain:

Thomas Graf potatoes

1kg potatoes

100 ml oyster sauce

1 clove of garlic (pressed)

1 tsp honey

Pinch of salt

Black pepper

1 tbsp oil

Wash the potatoes and cut them into wedges without peeling them. Add all the ingredients and mix well. Preheat the oven to 180°C, place the potatoes on a baking sheet and bake for 40 min.


PHOTO: Marietta Schupp/EMBL
PHOTO: Marietta Schupp/EMBL
PHOTO: Marietta Schupp/EMBL
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