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exploit the unique capabilities of the ID32 beamline. ID32 is a soft X-ray (400-1600eV) beamline with a scientific focus in the areas of electronic structure and magnetism. The beamline has two branches
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of colonial marine vertebrates (albatrosses, penguins, sea lions) reproduce in simple, structured communities, we are testing key hypotheses concerning the processes affecting the eco-epidemiological dynamics
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Inria, the French national research institute for the digital sciences | Paris 15, le de France | France | 2 months ago
Tollitte Changing Data Representation within the Coq System, Nicolas Magaud Changing Data Structures in Type Theory:A Study of Natural Numbers, Nicolas Magaud and Yves Bertot Where to apply Website https
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Institute of Molecular Mechanisms and Machines, (IMOL), Poland, and the Leicester Institute of Structural and Chemical Biology, United Kingdom. For more information about AMBER, visit: https
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structural data, which requires laboratory based as well as on-site analyses. The main objectives are as follows: Compile legacy data of stained glass windows, this requires extensive data curation and
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technique achieving an isotropic precision of 4 nm. The project builds on the integration of structured illumination to encode the axial position of single molecules into the phase of a modulated signal
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Energétique” Team at the SIAME Laboratory at UPPA in Pau. For more details on the activities of the laboratory's four teams (“Interactions Vagues-Structure” and “Géomatériaux et Structures” in Anglet and
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encoding of information, inspired by concepts from single-pixel imaging, and transposed to fluorescence microscopy through the use of structured illumination with variable frequency. The objective is to
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) - bibliographic survey (secondary task) - participating in the management of the laboratory (secondary task) Frame of the contract : the LHFA (https://www.lhfa.cnrs.fr/ ) is an Unité Mixte CNRS-Université de
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molecules using site-specific conjugation strategies. - Development of DNA origami scaffolds to spatially organize and orient proteins for structural studies by single-particle Cryo-Electron Microscopy