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by Lavkeshsharma at 10-06-2017, 03:36 AM
The 2017 chemistry laureates were recognised for developing cryo-electron microscopy. But what is it, why is it exciting and where will it take us next?

A trio of scientists share this year’s Nobel prize for chemistry: Jacques Dubochet, Joachim Frank and Richard Henderson.

Their win is for work on a technique known as cryo-electron microscopy that has allowed scientists to study biological molecules in unprecedented sharpness, not least the Zika virus and proteins thought to be involved in Alzheimer’s disease.

Being able to capture images of these biological molecules at atomic resolution not only helps scientists to understand their structures, but has opened up the possibility of exploring biological processes by stitching together images taken at different points in time. 

Cryo-electron microscopy has proved valuable in helping scientists to develop drugs.It has been used in visualising the way in which antibodies can work to stop viruses being dangerous, leading to new ideas for medicines as just one example.


Why do we need cryo-electron microscopy?

Microscopes allow scientists to look at structures that cannot be seen with the naked eye – but when these structures are very tiny, it is no longer possible to use rays of light to do the job because their wavelengths are not short enough. Instead, beams of electrons can be used – with a technique known as transmission electron microscopy (TEM) – or scientists can employ a method known as x-ray crystallography in which x-rays are scattered as they pass through samples, creating patterns that can be analysed to reveal the structure of molecules.

The trouble is, x-ray crystallography relies on biological molecules forming ordered structures, which many fail to do, and the technique does not allow researchers to probe how molecules move.

Historically, TEM also presented difficulties. The beam itself fried the biological molecules being studied, while the technique involved the use of a vacuum which resulted in biological molecules drying out and collapsing, throwing a spanner in the works when it came to probing their structure.

This year’s chemistry laureates tackled these conundrums, enabling scientists to use TEM to image biological molecules in incredible resolution.

What did they do?
Henderson and his team, using a glucose solution to prevent molecules drying out, combined a weaker beam of electrons with images taken from many angles and mathematical approaches to build up a 3D image of a protein neatly organised within a biological membrane. It was a breakthrough moment. Henderson later succeeded in unveiling its 3D structure at atomic resolution – a first for a protein.

Meanwhile Frank developed ingenious image processing techniques to unpick TEM data and build up images of biological molecules as they are in solution, where they point in many different directions.

Dubochet came up with a sophisticated approach to prevent molecules from drying out. Henderson’s technique did not work for water-soluble biological molecules, while freezing samples resulted in the formation of ice crystals which caused damage and made the resulting images challenging to interpret.

Dubochet’s solution was to rapidly cool samples at such speed that the water molecules did not have time to adopt a regular structure. Rather, they were left pointing every which way, resulting in a glass within which biological molecules were frozen in time – in their natural shape.

What’s next?

The trio’s work, and subsequent efforts to perfect these approaches, has already led to astonishing developments.The technique of cryo-TEM has really opened up the molecular world of the cell to direct observation.

Among the processes it has made clearer is the mechanism by which DNA is copied into the single-stranded molecule RNA. 

But the future is also exciting, with scientists using the technique to probe the structure of drug targets, as well as components within cells involved in sensing pain, temperature and pressure. Further improvements in resolution are also afoot.

Cryo-electron microscopy is one of those techniques so basic and important that its use spans all of biology – including understanding the human body and human disease and in designing new medicines.
by SunilNagpal at 10-05-2017, 05:18 AM
The Nobel Prize in Chemistry 2017 has been awarded to Jacques Dubochet, Joachim Frank and Richard Henderson "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution".

Prize amount: 9 million Swedish krona, to be shared equally between the Laureates.

Fllowing is the press release information as published on

Quote:A picture is a key to understanding. Scientific breakthroughs often build upon the successful visualisation of objects invisible to the human eye.

However, biochemical maps have long been filled with blank spaces because the available technology has had difficulty generating images of much of life’s molecular machinery.

Cryo-electron microscopy changes all of this. Researchers can now freeze biomolecules mid-movement and visualise processes they have never previously seen, which is decisive for both the basic understanding of life’s chemistry and for the development of pharmaceuticals.

Electron microscopes were long believed to only be suitable for imaging dead matter, because the powerful electron beam destroys biological material. But in 1990, Richard Henderson succeeded in using an electron microscope to generate a three-dimensional image of a protein at atomic resolution. This breakthrough proved the technology’s potential.

Joachim Frank made the technology generally applicable. Between 1975 and 1986 he developed an image processing method in which the electron microscope’s fuzzy twodimensional images are analysed and merged to reveal a sharp three-dimensional structure

Jacques Dubochet added water to electron microscopy. Liquid water evaporates in the electron microscope’s vacuum, which makes the biomolecules collapse. In the early 1980s, Dubochet succeeded in vitrifying water – he cooled water so rapidly that it solidified in its liquid form around a biological sample, allowing the biomolecules to retain their natural shape even in a vacuum.

Following these discoveries, the electron microscope’s every nut and bolt have been optimised. The desired atomic resolution was reached in 2013, and researchers can now routinely produce three-dimensional structures of biomolecules. In the past few years, scientific literature has been filled with images of everything from proteins that cause antibiotic resistance, to the surface of the Zika virus. Biochemistry is now facing an explosive development and is all set for an exciting future.

Attaching the Scientific Background of the research as well:

by vishu272 at 10-04-2017, 01:00 AM
Press Release


The Nobel Assembly at Karolinska Institutet has today decided to award

the 2017 Nobel Prize in Physiology or Medicine

jointly to

Jeffrey C. Hall, Michael Rosbash and Michael W. Young

for their discoveries of molecular mechanisms controlling the circadian rhythm
by samriti67 at 10-03-2017, 07:40 PM
Hi sir I'm BSc bt final yr student, I want to know jobs after graduation
by nikhila at 10-02-2017, 06:59 PM
Sir am currently a b tech 1st year student can u please suggest me some training programs,internships for me
by Lavkeshsharma at 10-01-2017, 07:56 PM
Links for GATE XL Question Papers from 2007 to 2017

GATE XL 2007

Organizer : IIT Kanpur

GATE XL 2008

Organizer : IISC Bangalore

GATE XL 2009

Organizer : IIT Roorkee

GATE XL 2010

Organizer : IIT Guhwati

GATE XL 2011

Organizer : IIT Madras

GATE XL 2012

Organizer : IIT Delhi

GATE XL 2013

Organizer : IIT Bombay

GATE XL 2014

Organizer : IIT Kharagpur

GATE XL 2015

Organizer : IIT Kanpur

GATE XL 2016

Organizer : IISC Bangalore

GATE XL 2017

Organizer : IIT Roorkee
by SunilNagpal at 10-01-2017, 02:05 AM
As per New York Academy of Sciences and CDC, modern world is suffering from the Sleep Deprivation epidemic. Everyone has a bare minimum requirement of sleep cycle to keep him/ her healthy. Here is a 2 min video that sheds light on the same.

Share it with everyone who you think badly needs some sleep in his / her life. Sleep well!!

by Fazlil at 09-30-2017, 05:20 PM
Why Gelatine doesn't absorb UV light at 280 mm?
by Fazlil at 09-30-2017, 02:26 PM
Sir I am a M.Sc Biotechnology 1st semester student of gauhati university. Has any scholarship for MSc biotechnology program
by Fazlil at 09-30-2017, 02:20 PM
Why Proline doesn't favour formation of alpha helix?
by Fazlil at 09-30-2017, 01:11 PM
Discuss the methods of determination of amino acid sequence of polypeptides.
by sanjanat at 09-30-2017, 03:55 AM
Who is this guy
Not giving his introduction and messageing on private no
by Lavkeshsharma at 09-29-2017, 11:36 PM
Urgently Required

Designation : Research Associate - Yeast Group

Job Responsibilities

- Thorough Knowledge and Execution of cloning.

- Maintenance of yeast strains

- PCR amplification.

- Media and buffer preparation.

- Extraction of Genomic DNA , RNA from Eukaryotes.

- Large and small scale plasmid preparation.


M.Sc. Biotechnology / Biochemistry / Microbiology / Life Sciences.


1 year academic or industrial experience.

Location : Manesar , Gurgaon

Interested candidates can share their CV's at careers @
by Fazlil at 09-29-2017, 07:22 PM
Why protiens are precipitated at their isoelectric point?
by ForumsEditor at 09-29-2017, 02:48 PM
Here are 10 some of the least known but amazing facts about human body in this short 1 minute video!

by Muskan Gupta at 09-29-2017, 02:08 PM
M I eligible for GATE biotechnology after BSc??....
by SunilNagpal at 09-29-2017, 05:49 AM

Following is the Abstract of this research that involves the precise base editing (also called Chemical Surgery of DNA) in Human Embryos for curing Thalassemia.

Titled: Correction of β-thalassemia mutant by base editor in human embryos

Abstract: β-Thalassemia is a global health issue, caused by mutations in the HBB gene. Among these mutations, HBB −28 (A>G) mutations is one of the three most common mutations in China and Southeast Asia patients with β-thalassemia. Correcting this mutation in human embryos may prevent the disease being passed onto future generations and cure anemia. Here we report the first study using base editor (BE) system to correct disease mutant in human embryos. Firstly, we produced a 293T cell line with an exogenous HBB −28 (A>G) mutant fragment for gRNAs and targeting efficiency evaluation. Then we collected primary skin fibroblast cells from a β-thalassemia patient with HBB −28 (A>G) homozygous mutation. Data showed that base editor could precisely correct HBB −28 (A>G) mutation in the patient’s primary cells. To model homozygous mutation disease embryos, we constructed nuclear transfer embryos by fusing the lymphocyte or skin fibroblast cells with enucleated in vitro matured (IVM) oocytes. Notably, the gene correction efficiency was over 23.0% in these embryos by base editor. Although these embryos were still mosaic, the percentage of repaired blastomeres was over 20.0%. In addition, we found that base editor variants, with narrowed deamination window, could promote G-to-A conversion at HBB −28 site precisely in human embryos. Collectively, this study demonstrated the feasibility of curing genetic disease in human somatic cells and embryos by base editor system.

Read the entire research at Journal of Protein & Cell
by Abhijeeth Nair at 09-28-2017, 02:57 PM
i want to be a genetical engineer and i completed my 12 class with aggregate of 77% what i have to do now plzz help me...
by Lavkeshsharma at 09-28-2017, 03:15 AM
Links for GATE BT Question Papers from 2010 to 2017
( GATE BT was first organized in 2010 )

GATE BT 2010 :

Organizer : IIT Guhwati

GATE BT 2011 :

Organizer : IIT Madras

GATE BT 2012 :

Organizer : IIT Delhi

GATE BT 2013 :

Organizer : IIT Bombay

GATE BT 2014 :

Organizer : IIT Kharagpur

GATE BT 2015 :

Organizer : IIT Kanpur

GATE BT 2016 :

Organizer : IISC Bangalore

GATE BT 2017 :

Organizer : IIT Roorkee
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