Tuesday 8 March 2016

High throughput computing helps LIGO confirm Einstein’s last unproven theory

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A few years ago, a global team of scientists parlayed decades of research into the discovery of the Higgs boson. A humble software program called HTCondor churned away in the background, helping analyze data gathered from billions of particle collisions. Cut to 2016, and HTCondor is on to a new collision: helping scientists detect gravitational waves caused 1.3 billion years ago by a collision between two black holes 30 times larger than our sun.
via Science Daily
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Innovative catalyst fabrication method may yield breakthrough in fuel cell development

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Researchers working on developing new fuel cells have published a novel method to fabricate highly active gold nanoparticle catalysts. The team adopted methods it had already proven with platinum, and a polymer was wrapped around graphene to create an ideal support structure for the nanoparticles. The catalysts showed best-in-class results in what may become a breakthrough technology for the key catalytic reaction in fuel cells.
via Science Daily

Showcasing high-energy women

Simulation analyzes cosmic rays

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When cosmic rays hit the Earth’s atmosphere, their high-energy primary particles generate an “air shower” of secondary particles. These cascades of particles provide information on the physical properties of the primary particles, the origin of which has been studied by astrophysicists for generations. Measurements of LOFAR (Low Frequency Array), the biggest radio telescope worldwide, provide new findings on the mass and potential sources of the particles.
via Science Daily
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First tomatoes, peas harvested on Mars, moon soil simulant

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The second experiment on how to grow crops on Mars and moon soil simulant have given a surprising outcome. As a result of what the researchers in the Netherlands learned from their first experiments, they were able to grow ten different crop species. Tomatoes, peas, rye, garden rocket, radish and garden cress were harvested.
via Science Daily
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Solar Eclipse Shoes in the Classroom

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The total solar eclipse of March 8/9 will be the only total eclipse in 2016. The New Moon's dark shadow traces a limited, narrow path across planet Earth for viewing the total phase, making landfall in Indonesia and mostly tracking across the Pacific Ocean. A much larger region will be witness to a partially eclipsed Sun though, and safely viewing the eclipse can actually be very easy. One technique is demonstrated in this shoe group portrait from a classroom in Rosenfeld, Germany, taken during March 2015's solar eclipse. With blinds closed to darken the room, each threaded hole in the window blind creates a pinhole camera, projecting multiple images of the eclipsed sun that march across the floor. Other viewing alternatives include eclipse glasses and a comfortable chair, but be sure to wear a fashionable eclipse shirt.

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Graphene sheets enable single protein snapshots

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Taking pictures of single proteins is an important goal in biology and medicine, allowing the study of protein folding and other behavior, and possibly leading to new approaches in drug development. Imaging single proteins, however, requires high-intensity electron beams or x-ray sources, which necessarily damage the protein. An alternative is to use low-intensity radiation for imaging, however then the exposure time has to increase and the proteins tend to drift away from the photo. Now Jean-Nicolas Longchamp and colleagues at the University of Zurich in Switzerland have used Graphenea’s CVD graphene as a transparent trap that holds proteins in place while they’re imaged with a low-energy electron beam. We caught up with Jean-Nicolas for a few words about the result.

1) How does your protein imaging technique work?

Our imaging technique is called low-energy electron holography. In the experiment, a sharp metal tip acts as a source of highly coherent electrons. The atomic sized electron emitter is brought as close as 100nm to the sample with nanopositioning. Part of the electron wave is elastically scattered off the object and hence is called the object wave, while the un-scattered part of the wave represents the reference wave. At a distant detector, the hologram, i.e. the pattern resulting from the interference of these two wave fronts is recorded. A hologram, in contrast to a diffraction pattern, contains the phase information of the object wave, and the object structure can thus be reconstructed easily and unambiguously.

2) How does graphene help the imaging?

In order to enable the imaging, the proteins need to be deposited onto a transparent and conductive substrate for low-energy electrons. We could show that ultraclean freestanding graphene is highly transparent (more than 70%) for those electrons. To attain such high transparency, the graphene samples were prepared by our patented method based on the catalytic activity of Pt-metal. While until today, solely graphene has been demonstrated to be a suitable substrate for low-energy electron holography, we are trying to prepare other 2D materials (as for instance h-BN) and 2D-heterostructures in an ultraclean freestanding manner to investigate their properties.

3) What's the significance of the particular proteins you used in this study? What's the immediate medical application?

Currently, we are in the process of developing our imaging technique for structural biology purposes, with the goal of imaging individual proteins at atomic resolution. For that, we are now imaging proteins whose structures are already known from X-ray crystallography investigations and compare our images to the proposed atomic models. We are sure that once we have attained atomic resolution, the pharmaceutical industry would be very interested in images of proteins with unknown structures, in particular proteins which could not be crystallized. Images of individual proteins at atomic resolution will deliver very important information for the design of novel and better drugs.

4) How does your method fare against other protein imaging techniques?

Most of the protein structural information available today has been obtained from either X-ray crystallography experiments or cryo-electron microscopy investigations by means of averaging over many molecules assembled into a crystal or over a large ensemble selected from low signal-to-noise ratio electron micrographs respectively. Despite the impressive amount of available data, a strong desire for acquiring structural data from just one individual molecule is emerging for good reasons. Most of the biologically relevant molecules exhibit different conformations; the associated structural details however, remain undiscovered when averaging is involved. Moreover, a large subset of the entirety of proteins, in particular out of the important category of membrane proteins, does not crystallize at all. If just one individual protein or protein complex can be analyzed in sufficient detail, also those objects become accessible.

For a meaningful contribution to structural biology, a tool for single molecule imaging has to allow for observing an individual protein long enough to acquire a sufficient amount of data for revealing its structure, ideally without destroying it. The strong inelastic scattering cross-section for both X-rays and high-energy electrons as employed in state-of-the-art aberration corrected TEMs, inhibits accumulation of sufficient elastic scattering events required in order to reveal high-resolution reconstruction of just one molecule. Future X-ray Free Electron Lasers (FELs) with drastically enhanced brightness and reduced pulse duration might eventually achieve the goal of single molecule imaging. Yet, the current and foreseeable state-of-the-art in FEL performance still requires averaging over at least 1 million molecules.

In contrast to this, biomolecules as for instance DNA or proteins withstand irradiation by low-energy electrons and remain unperturbed even after a total dose of at least 5 orders of magnitude larger than the permissible dose in X-ray or high-energy electron imaging. The damage-free radiation of low-energy electrons combined with the fact that the de Broglie wavelengths associated with this energy range are of the order of 1Å, make low-energy electron holography an auspicious candidate for structural biology at the single molecule level.

5) What's next for this project?

The next goal for this project is to attain atomic resolution imaging of individual proteins. For that, a low-energy electron holographic microscope capable of operation at cryogenic temperatures while keeping very high mechanical stability, which is mandatory for holography, needs to be designed and implemented.

Thank you Jean for your time.


via Graphenea

A perfectly still laboratory in space

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Following a long series of tests, ESA’s LISA Pathfinder has started its science mission to prove key technologies and techniques needed to observe gravitational waves from space.


via ESA Space Science
http://www.esa.int/Our_Activities/Space_Science/A_perfectly_still_laboratory_in_space

Citizen scientists help NASA researchers understand auroras

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Aurorasaurus is a citizen science project that tracks auroras through the project's website, mobile apps and Twitter.
via Science Daily
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Ultra-bright light: A new source of quantum light

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A new ultra-bright source of single photons - 15 times brighter than commonly used sources and emitting photons that are 99.5% indistinguishable from one another - has been developed.
via Science Daily