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Field
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ICFO is offering a postdoctoral position to a well-qualified, highly motivated and dynamic young scientist who wishes to enhance his/her scientific career in a friendly and stimulating environment. The successful candidate will be joining the Ultracold Quantum Gases group led by Prof. Dr.Leticia...
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The CFN is seeking an exceptional Postdoctoral Research Associate to conduct research directed to developing state-of-the-art electron microscopy techniques particularly to probe amorphous materials
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background in biophysics, with a focus on ion channel research. Prior experience with patch-clamp electrophysiology and advanced microscopy techniques is highly desirable. The Dai lab investigates
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to study this question. Candidates should have a good publication record and Ph.D. in neuroscience. Experience with neuroanatomy, advanced microscopy, mouse behavior and electrophysiology are desired. Other
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: bacteriology, fluorescence microscopy, electron microscopy, antibiotic assays, biochemical purifications, biochemical assays such as binding assays and protein gel electrophoresis, as well as analytical methods
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focused on advanced tissue imaging for diagnostic and intraoperative applications. The successful candidate will work on federally funded projects aimed at developing and applying novel microscopy platforms
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-mechanical testing of interfaces in multilayered films across a wide range of temperatures (cryogenic to elevated temperatures) and strain rates using in situ SEM techniques Electron microscopy-based
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Nanophysics group has an intense activity on the use of atomic force microscopy techniques to probe and map functionalities at the nanoscale, with a particular emphasis on piezoresponse force microscopy (PFM
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strongly interdisciplinary. Specifically, our star technique is scanning electrochemical cell microscopy (SECCM) , a powerful electrochemical imaging technique for interrogating electrochemical processes
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microscopy) studies that have begun to define the molecular basis for MX2’s interaction with the HIV-1 capsid lattice, and the disruptive sequelae of binding – for capsid structure, virion particle integrity