Life Sciences

Pharmaceutical companies and academic researchers are making increasing use of a synchrotron technique called macromolecular crystallography, which is used to solve the 3D structure of important biomolecules such as proteins. Chemists and structural biologists use this method to work together in the development of promising compounds into drug candidates.

Synchrotrons can also help us to better understand diseases which involve a change in the fold of a protein, so that the protein becomes pathogenic (for example Creutzfeld-Jacob-Desease (CJD), Alzheimer's Disease, BSE).

New foot-and-mouth vaccine signals huge advance in global disease control

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Diamond Light Source, Oxfordshire, UK

Scientists have developed a new methodology to produce a vaccine for foot-and-mouth disease virus (FMDV). Because the vaccine is all synthetic, made up of tiny protein shells designed to trigger optimum immune response, it doesn’t rely on growing live infectious virus and is therefore much safer to produce.  

Furthermore, these empty shells have been engineered to be more stable; making the vaccine much easier to store and reducing the need for a cold chain. This is important research because it represents a big step forward in the global campaign to control FMDV in countries where the disease is endemic, and could significantly reduce the threat to countries currently free of the disease. Crucially, this new approach to making and stabilising vaccine could also impact on how viruses from the same family are fought, including polio.

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Research Reveals Rapid DNA Changes that Act as Molecular Sunscreen

Thymine – the molecule in the foreground – is one of the four basic building blocks that make up the double helix of DNA. It’s such a strong absorber of ultraviolet light that the UV in sunlight should deactivate it, yet this does not happen. In a study reported in Nature Communications, researchers used an X-ray laser at SLAC National Accelerator Laboratory to make detailed observations of a “relaxation response” that protects these molecules, and the genetic information they encode, from UV damage.
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Thymine – the molecule in the foreground – is one of the four basic building blocks that make up the double helix of DNA. It’s such a strong absorber of ultraviolet light that the UV in sunlight should deactivate it, yet this does not happen. In a study reported in Nature Communications, researchers used an X-ray laser at SLAC National Accelerator Laboratory to make detailed observations of a “relaxation response” that protects these molecules, and the genetic information they encode, from UV damage.

Linac Coherent Light Source, SLAC National Accelerator Laboratory, California, USA

The molecular building blocks that make up DNA absorb ultraviolet light so strongly that sunlight should deactivate them - yet it does not. Now scientists have made detailed observations of a "relaxation response" that protects these molecules, and the genetic information they encode, from UV damage. The experiment at the U.S. Department of Energy's SLAC National Accelerator Laboratory focused on thymine, one of four DNA building blocks. Researchers hit thymine with a short pulse of ultraviolet light and used the LCLS' powerful X-ray laser to watch the molecule's response: A single chemical bond stretched and snapped back into place within 200 quadrillionths of a second, setting off a wave of vibrations that harmlessly dissipated the destructive UV energy.

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The malaria parasite under a super microscope

Structure of the plasmodium protein actin I (red). Replacing the D-loop in subdomain 2 (circled) with that of vertebrate muscle actin causes actin I to form long filaments (grey and background) instead of the usual short oligomers.
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Structure of the plasmodium protein actin I (red). Replacing the D-loop in subdomain 2 (circled) with that of vertebrate muscle actin causes actin I to form long filaments (grey and background) instead of the usual short oligomers.

PETRA III, DESY, Hamburg, Germany

An international team of scientists has decoded two key proteins of the malaria parasite Plasmodium, using DESY's bright X-ray source PETRA III and other facilities. The results shed light on the workings of Plasmodium's structural proteins actin I and actin II, without which the parasite cannot infect human cells. The project led by Prof. Inari Kursula from the new Centre for Structural Systems Biology (CSSB) on the DESY campus may contribute to the development of tailor-made drugs against malaria.

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Fatty Acid Biosynthesis Caught in the Act

Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, California, USA

Fatty acids are key components of a variety of biological functions ranging from cellular membranes to energy storage. In addition, they are of great interest as potential "green" biofuels and targets in the development of novel antibiotics. In order to fully exploit their potential, researchers must first understand in detail how organisms synthesize fatty acids. However, due to the dynamic nature of the process, structural and functional studies of fatty acid biosynthesis are very challenging. A team of scientists has recently made a giant leap forward by determining the structure of a protein-protein complex that represents a snapshot of fatty acid biosynthesis in action.

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