SLAC National Accelerator Laboratory
Showing 1,901-2,000 of 2,124 Results
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Lokman (Robin) Turkmen
Project Manager - Fac/Const, SLAC National Accelerator Laboratory
Current Role at StanfordI am currently working for SLAC National Accelerator Laboratory which operated by Stanford University as a contractor for the United States Department of Energy (DOE) in San Francisco Bay Area as Senior Project Manager.
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MANUEL RAFAEL VEJAR
Postdoctoral Scholar, Photon Science, SLAC
BioManuel (Manny) Vejar is a postdoctoral scholar at SLAC National Accelerator Laboratory, specializing in synchrotron X-ray fluorescence imaging and X-ray absorption spectroscopy to study environmental and rhizosphere biogeochemistry at the Stanford Synchrotron Radiation Lightsource.
He received his Ph.D. in the Civil & Environmental Engineering & Earth Sciences department at the University of Notre Dame in 2024. His doctoral research focused on the impacts of iron-oxide mineral complexity on the fate and transport of plutonium in nuclear waste repository and/or legacy environmental contamination settings. Specifically, he studied the influence of Al-substitution in iron (oxyhydr)oxide minerals on the redox and speciation behavior of plutonium at the mineral-water interface, employing M4-edge high-energy resolution fluorescence-detected X-ray absorption near-edge structure (HERFD-XANES) spectroscopy to determine the oxidation state and L3-edge extended X-ray absorption fine-structure (EXAFS) spectroscopy to determine coordination environment of the plutonium associated with these minerals.
He has over 7 years of experience with synchrotron techniques (micro-X-ray fluorescence imaging, XANES, and EXAFS), and their applications to study metal(loid)s in environmental systems. During his career, Manny has conducted work at the Stanford Synchrotron Radiation Lightsource, the Advanced Photon Source, and the European Synchrotron Radiation Facility, while collaborating with Chapman University, the Institute of Resource Ecology at the Helmholtz-Zentrum Dresden-Rossendorf, and more recently Oak Ridge, Pacific Northwest, and Livermore national labs, and the University of Puerto Rico in Mayaguez. Prior to his Ph.D. at the University of Notre Dame, Manny obtained his B.Sc. in Geology from the California State Polytechnic University, Pomona. -
Caterina Vernieri
Assistant Professor of Particle Physics and Astrophysics
BioCaterina Vernieri received her PhD on the CMS experiment from the Scuola Normale Superiore in Pisa, Italy, in 2014 and then moved to Chicago for a postdoctoral fellowship at the Fermi National Accelerator Laboratory. She joined SLAC in 2018 as a Panofsky Fellow and moved to the ATLAS experiment, and in 2022 she became Assistant Professor.
Throughout this time, she has been devoted to studying the Higgs boson using data from the LHC. She co-led the group in the CMS experiment studying the Higgs decay to b quarks at the time that this important decay process was finally discovered in the data. At SLAC, Caterina is working with the ATLAS experiment at the LHC with a focus on Higgs physics. She is responsible for the integration activities at SLAC of the new ATLAS Pixel Inner Tracker detector.
She was also co-convener of the group on Higgs boson properties in the US national study of the future of particle physics. -
Johannes Voss
Staff Scientist, SLAC National Accelerator Laboratory
BioJohannes Voss is Staff Scientist at the SUNCAT Center for Interface Science and Catalysis at SLAC National Accelerator Laboratory. He leads a research team focused on the atomic-level understanding and computational design of systems of relevance for renewable storage and conversion of energy. The team employs data-scientific approaches to improve the predictive power of super computer simulations for chemical reactions with emphasis on heterogeneous catalysis.
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Soichi Wakatsuki
Professor of Photon Science and of Structural Biology
Current Research and Scholarly InterestsUbiquitin signaling: structure, function, and therapeutics
Ubiquitin is a small protein modifier that is ubiquitously produced in the cells and takes part in the regulation of a wide range of cellular activities such as gene transcription and protein turnover. The key to the diversity of the ubiquitin roles in cells is that it is capable of interacting with other cellular proteins either as a single molecule or as different types of chains. Ubiquitin chains are produced through polymerization of ubiquitin molecules via any of their seven internal lysine residues or the N-terminal methionine residue. Covalent interaction of ubiquitin with other proteins is known as ubiquitination which is carried out through an enzymatic cascade composed of the ubiquitin-activating (E1), ubiquitin-conjugating (E2), and ubiquitin ligase (E3) enzymes. The ubiquitin signals are decoded by the ubiquitin-binding domains (UBDs). These domains often specifically recognize and non-covalently bind to the different ubiquitin species, resulting in distinct signaling outcomes.
We apply a combination of the structural (including protein crystallography, small angle x-ray scattering, cryo-electron microscopy (Cryo-EM) etc.), biocomputational and biochemical techniques to study the ubiquitylation and deubiquitination processes, and recognition of the ubiquitin chains by the proteins harboring ubiquitin-binding domains. Current research interests including SARS-COV2 proteases and their interactions with polyubiquitin chains and ubiquitin pathways in host cell responses, with an ultimate goal of providing strategies for effective therapeutics with reduced levels of side effects.
Protein self-assembly processes and applications.
The Surface layers (S-layers) are crystalline protein coats surrounding microbial cells. S-layer proteins (SLPs) regulate their extracellular, self-assembly by crystallizing when exposed to an environmental trigger. We have demonstrated that the Caulobacter crescentus SLP readily crystallizes into sheets both in vivo and in vitro via a calcium-triggered multistep assembly pathway. Observing crystallization using a time course of Cryo-EM imaging has revealed a crystalline intermediate wherein N-terminal nucleation domains exhibit motional dynamics with respect to rigid lattice-forming crystallization domains. Rate enhancement of protein crystallization by a discrete nucleation domain may enable engineering of kinetically controllable self-assembling 2D macromolecular nanomaterials. In particular, this is inspiring designing robust novel platform for nano-scale protein scaffolds for structure-based drug design and nano-bioreactor design for the carbon-cycling enzyme pathway enzymes. Current research focuses on development of nano-scaffolds for high throughput in vitro assays and structure determination of small and flexible proteins and their interaction partners using Cryo-EM, and applying them to cancer and anti-viral therapeutics.
Multiscale imaging and technology developments.
Multimodal, multiscale imaging modalities will be developed and integrated to understand how molecular level events of key enzymes and protein network are connected to cellular and multi-cellular functions through intra-cellular organization and interactions of the key machineries in the cell. Larger scale organization of these proteins will be studied by solution X-ray scattering and Cryo-EM. Their spatio-temporal arrangements in the cell organelles, membranes, and cytosol will be further studied by X-ray fluorescence imaging and correlated with cryoEM and super-resolution optical microscopy. We apply these multiscale integrative imaging approaches to biomedical, and environmental and bioenergy research questions with Stanford, DOE national labs, and other domestic and international collaborators. -
Faya Wang
Lead Scientist, SLAC National Accelerator Laboratory
Bio• 20-year scientific career in academia and national lab
• Pursuing research leadership position in high-impact cutting-edge tech organization
• Extensive hands on experience on particle accelerator and rf system
• Electron beam dynamics, beam optics, control system dynamics, accelerator design, electrodynamics, electromagnetic field, high power microwave system, beam and rf diagnostics, electromagnetic field design
