a brief overview on Nobel prize in chemistry 2017.. JoachimFrankJacques Dubochet RICHARD HENDERSON

3. JoachimFrankJacques Dubochet RICHARD
HENDERSON

4.  1950s,Cambridge university exposed
protein crystals to x-ray beams-(wavy
structure)
 1980s,x-ray crystallography & NMR-
Reveals protein structure.
 Introduction of transmission electron
microscope.

5. • Requires vacuum, surrounding water evaporates.
• Biomolecules dry out, they collapse and loss their natural
structure making images useless.
• The intense electron beam necessary for obtaining high
resolution images incinerates biological material and, if the
beam is weakened, the image loses its contrast and
becomes fuzzy.

6. Allows the observation of specimens that have
not been stained or fixed in any way.
Showing them in their native environment.
Less in functionally irrelevant conformational
changes.
No need of protein crystals.

7. 7

8. 8

9. 9
 A Form of EM; sample is studied at Cryogenic
Temperatures(-150 ° C)
 Native state of specimen; not stained not Fixed
 Specimens are observed in vitreous ice
 Cryo-fixation; Rapid freezing of
sample.

10. Involved in Cryo-EM
10

11. 10Schematic Diagram of Cryo-EM

12. Structure of Hepatitis B Virus Solved by
Cryo-EM
12

13. 13
 Nanoparticle Research
 Pharmaceutical Drug Research
 3D Structure Visualization of:
 Single Particles such as Ribosome, tRNA
 Viruses
 Proteins
 Macromolecules; Lipid Vesicles

14. 14
 A number of improvements are expected in future
 High Voltage Electron Source
 Mathematical Correction of Lens Defects
 High Resolution
 Improved Scanners
 Better High-Pressure Freezing
 Improved CCD detectors will remove the need for computer
processing in future

16. • Born 19 July 1945 (age 72) Edinburgh,
Scotland
• Education University of Edinburgh (BSc)
• Darwin College, Cambridge (PhD)
• Known for Single-particle cryo-electron microscopy
• Awards Nobel Prize in Chemistry (2017)
• Scientific career
• Fields Structural biology and Cryo-electron microscopy
• Institutions Laboratory of Molecular Biology

17. • bacteriorhodopsin structure at
atomic resolution.
The first rough model of
bacteriorhodopsin

18. • Born 12 September 1940 (age 77) Siegen,
• Germany
• Education University of Freiburg (BS)
University of Munich (MS), Max Planck Society
Technical University of Munich (PhD)
• Known for Single-particle cryo-electron microscopy Ribosome structure and
dynamics
• Awards Benjamin Franklin Medal in Life Science (2014),Wiley Prize in
Biomedical Sciences (2017),Nobel Prize in Chemistry (2017)
• Scientific career
• Fields Structural biology and Cryo-electron microscopy
• Institutions Columbia University College of Physicians and Surgeons,
Department of Biochemistry and Molecular Biophysic

20. • Born 8 June 1942 (age 75)
• Aigle, Switzerland
École polytechnique fédérale de Lausanne (BS)
• University of Geneva (MS)
• University of Geneva (PhD)
Cryo-electron microscopy
• Awards Nobel Prize in Chemistry (2017)
• Scientific career
• Fields Structural biology
• Cryo-electron microscopy
• Institutions European Molecular Biology Laboratory (1978-1987)
University of Lausanne (since 1987)

23. 23
 Cryo-EM is a form of Transmission Electron Microscopy (TEM)
where the sample is studied in its native state at cryogenic
temperatures
 Used for 3D visualization of biological molecules
 Resolution of Cryo-EM is not high enough but it is improving using
different computer techniques
 With the advancement of technology, this technique will certainly
improve

24. 24
• Cryo-electron microscopy, Methods in Molecular Biophysics, Spring 2009
• Cryo-electron microscopy: taking back the knight Stephen Fullerpy,
MICROBIOLOGYTODAY VOL 26/MAY 99
• http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2678009/pdf/nihms87373.pdf
http://www.bbc.co.uk/dna/hub/A914302#back10
http://www.physorg.com/news192189631.html http://en.wikipedia.org/wiki/Cryo-
electron_microscopy http://www.jic.ac.uk/microscopy/intro_EM.html
• http://en.wikibooks.org/wiki/Structural_Biochemistry/Proteins/Cryo-
Electron_Microscopy
• http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2726835/pdf/nihms100338.pdf








