{"id":15462,"date":"2015-07-09T08:51:00","date_gmt":"2015-07-09T08:51:00","guid":{"rendered":"https:\/\/www.embl.org\/about\/info\/alumni\/?p=15462"},"modified":"2022-09-06T08:55:57","modified_gmt":"2022-09-06T08:55:57","slug":"2015-lennart-philipson-award","status":"publish","type":"post","link":"https:\/\/www.embl.org\/about\/info\/alumni\/blog\/2015\/07\/2015-lennart-philipson-award\/","title":{"rendered":"2015 Lennart Philipson Award"},"content":{"rendered":"\n

It\u2019s the one time of year when the EMBL community gets together in one place to celebrate scientific achievements, the Laboratory\u2019s unique spirit, and draw inspiration from friends and colleagues. And one of the highlights of Lab Day, which took place on 10 July, is where EMBL celebrates the very special work of alumni through the John Kendrew and Lennart Philipson awards<\/a>. We caught up with this year\u2019s winner of the Lennart Philipson Award to find out more.<\/p>\n\n\n\n

Science, society & serendipity<\/h3>\n\n\n\n
\"\"
Iain Mattaj with Jacques Dubochet<\/figcaption><\/figure><\/div>\n\n\n\n

As a child, alumnus Jacques Dubochet was scared of the dark. One day, nervously watching the sun disappearing over the horizon, he headed to his local library determined to find out where it went.<\/p>\n\n\n\n

\u201cFor me it was necessary to confront my fears with understanding,\u201d explains Dubochet, winner of the inaugural Lennart Philipson award. Taking comfort in knowledge instinctively led him to a career in science, where his defining work came not from studying disappearing light, but disappearing water, developing a technique that revolutionised structural biology.<\/p>\n\n\n\n

Friend not foe<\/h3>\n\n\n\n

\u201cUnfortunately water evaporates in an electron microscope, but when treated with suitable care, water is the electron microscopist\u2019s best friend,\u201d says Dubochet, who together with colleague Alasdair McDowall and Marc Adrian, invented cryo-electron microscopy (cryo-EM) sample preparation. The method enabled samples to be kept in their native state without the need for dyes or fixatives: its development over time has enabled researchers to zoom in on structures, viruses and protein complexes at unprecedented resolution. \u201cElectrons are great: even a single molecule may leave a trace in their beam and electron microscopists have learned to make use of them with breathtaking effect,\u201d he explains. \u201cBut they are also rather destructive: the column of an electron microscope must be under a vacuum, while risks of structural damage lurk around every corner.\u201d<\/p>\n\n\n\n

Scientists, including Dubochet had already tinkered with a variety of methods to try and fix biological samples for observations in the electron microscope, but working as a group leader at EMBL Heidelberg in the early 1980s, Dubochet recognised that in order to preserve the natural structure of biological samples for measurement under the electron microscope, they had to remain in their natural environment \u2013 water. But to avoid evaporation in the vacuum of the electron microscope column water needs to be frozen, with ice crystals causing further hazards to delicate samples. So Dubochet set out to find a way of freezing water without producing any ice crystals.<\/p>\n\n\n\n

Visionary<\/h3>\n\n\n\n

\u201cJacques had a vision,\u201d explains Gareth Griffiths, incumbent Chair of EMBL\u2019s Alumni Association, as well as a friend and colleague. \u201cHe found a way of freezing thin films of water so fast that crystals had no time to form. At first the idea of \u201cvitrification\u201d of liquid ice was dismissed, but overtime the technique has become increasingly important to life science research, and it is clear today it is Nobel Prize-worthy.\u201d While other structural biology methods require extensive, complicated and potentially disruptive sample preparation techniques, cryo-electron microscopy enables the scientist to view the sample in its natural environment. It is central to the work of labs the world over, including several at EMBL, while cryoEM of vitreous sections (CEMOVIS), is widely regarded as having potential to become a powerful method in the future. \u201cWith a bit of chance it\u2019s going to be trivial to see the atomic structure of protein complexes!\u201d Dubochet says excitedly.<\/p>\n\n\n\n

After leaving EMBL, Dubochet took up a professorship at the University of Lausanne, fulfilling a passion for teaching, while also introducing courses on ethics and philosophy- an area he is still very active in. \u201cWith knowledge comes great responsibility,\u201d he says. Now retired, he looks back with a smile at all he has achieved and experienced. \u201cI have been lucky,\u201d he adds. \u201cAlthough \u2018serendipity\u2019 probably captures it better, being in the right place at the right time. EMBL was the best time of my life: my children were born, I had my best scientific moments and still have plenty of friends here. We often come back to visit, it\u2019s a great pleasure. Voila!\u201d<\/p>\n\n\n\n

By Rosemary Wilson and Adam Gristwood<\/em><\/p>\n","protected":false},"excerpt":{"rendered":"

It\u2019s the one time of year when the EMBL community gets together in one place to celebrate scientific achievements, the Laboratory\u2019s unique spirit, and draw inspiration from friends and colleagues. And one of the highlights of Lab Day, which took place on 10 July, is where EMBL celebrates the…<\/p>\n","protected":false},"author":16,"featured_media":15466,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[1],"tags":[],"embl_taxonomy":[],"class_list":["post-15462","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-general"],"acf":[],"embl_taxonomy_terms":[],"featured_image_src":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-content\/uploads\/2022\/09\/dubochet_ov.png","_links":{"self":[{"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/posts\/15462","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/users\/16"}],"replies":[{"embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/comments?post=15462"}],"version-history":[{"count":7,"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/posts\/15462\/revisions"}],"predecessor-version":[{"id":15482,"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/posts\/15462\/revisions\/15482"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/media\/15466"}],"wp:attachment":[{"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/media?parent=15462"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/categories?post=15462"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/tags?post=15462"},{"taxonomy":"embl_taxonomy","embeddable":true,"href":"https:\/\/www.embl.org\/about\/info\/alumni\/wp-json\/wp\/v2\/embl_taxonomy?post=15462"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}