Nobel Prize in Chemistry: Big Mikrobenkino

How do salmonella body cells inject poison? Thanks to the frosty Kryomikroskopie you can see that. and thus smallest structures of life. That deserves the Nobel Prize.

Nobel Prize in Chemistry: Big Mikrobenkino
Content
  • Page 1 — Big Mikrobenkino
  • Page 2 — what holds molecules toger in innermost
  • Read on a page

    This technique is literally cool – cryo level. With Kryoelektronenmikroskopen, researchers capture atomic details of life – cells, viruses and molecules of individual proteins. Such filigree structures cannot be easily identified under an electron microscope. The radiation y were exposed to would destroy m. But well cooled – shock frosted so to speak – sensitive ramifications are protected and become visible.

    Without Jacques Dubochet, Joachim Frank and Richard Henderson, this would not have been possible. This is exactly why three researchers are receiving Nobel Prize in chemistry this year.

    "A revolutionary technique" is Kryoelektronenmikroskopie, says Thomas Marlovits. He leads Institute of Structural and System biology at university Eppendorf in Hamburg and works himself with such microscopes. The fact that re was now a Nobel Prize for this is particularly pleasing to him. "In Stockholm at press conference, Nobel jury even showed our images of needle complexes of salmonella attacking cells," says Marlovits. He's investigating pathogens. Only since re are such microscopes can his working group see what y do at molecular level exactly.

    © Moritz Küstner Dagny Lüdemann Head of department group knowledge and digital at time online to author page

    The foundations for this are from fresh Nobel laureates. The German-American biophysicist Joachim Frank first created three-dimensional recordings under an electron microscope. Between 1975 and 1986, with a specially sophisticated image processing method, he added up to n common 2-D shots to new images. In 1980s, his colleague, Swiss Jacques Dubochet, developed a method that made it possible to freeze samples from living material without destroying m. The Scottish biologist Richard Henderson finally created 1990 first 3-D image of a single protein.

    Gently shoot with electrons

    But how exactly does Kryomikroskopie, which has become a common practice since its last major development in year 2013? At minus 180 degrees Celsius or less, objects you want to observe are cooled down extremely quickly. "We can look at different states of a molecule – and do not need dyes anymore", explains Marlovits. When researchers used to determine structures of molecules of a salmonella or a piece of DNA, y first had to crystallize it. Because only n was it stable and literally hardened against aggressive rays.

    The final technical hurdle was overcome in 2013, when a new type of electron detector came into use. Pic.twitter.com/Ue9c0R6v7y

    — The Nobel Prize (@NobelPrize) October 4, 2017

    A complicated procedure in which you had to treat a lot of molecules with all kinds of salts and solutions, until desired crystals formed due to some of m – by chance. This could n be irradiated with X-rays and a picture calculated from data. The preserved images show molecules only in a certain state. A little bit as if you wanted to understand tactics in a football game and would only have a pile of snapshots. On each of same picture: How a foot hits a ball.

    In blast of microscopy, however, different moments can be frozen. To stay in picture, you would see a running striker, a goalkeeper or a blocking defensive player after ball. Back in molecular biology, this means: If you look at DNA or or molecules using this method, you will find snapshots of how, for example, a section of genetic is being copied, anor snapshot of how proteins Cut out a little bit and so on.

    Date Of Update: 05 October 2017, 12:07
    NEXT NEWS