SLAC National Accelerator Laboratory


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  • Aaron Roodman

    Aaron Roodman

    Professor of Particle Physics and Astrophysics

    BioAaron Roodman is a professor of Particle Physics & Astrophysics at Stanford’s SLAC National Accelerator Laboratory. Trained in experimental particle physics, he spent two decades studying differences between Matter and antiMatter, before turning his research to astrophysics and cosmology. Roodman’s current research focuses on the study of Dark Energy using images from large optical telescope surveys, such as the Dark Energy Survey and the upcoming Legacy Survey of Space and Time. He is also responsible for the assembly and testing of the world’s largest digital camera, the Vera C. Rubin Observatory's LSST Camera.

  • Philip Schuster

    Philip Schuster

    Professor of Particle Physics and Astrophysics

    BioProfessor Schuster is a theoretical physicist focused on identifying dark matter and its properties, developing concepts for new experimental tests of physics beyond the Standard Model, and studying novel theories of long-range forces. He is also directly involved in several experimental efforts as co-spokesperson for APEX, a founding member and physics coordinator for LDMX, and as a founding member of HPS.

    Prospective graduate students interested in research rotations should contact Professor Schuster directly. Recent research directions include new ideas to detect axions, milli-charge dark matter, the use of novel accelerator experiments to search for light WIMP-like dark matter, and generalizations of gauge theories that include massless particles with continuous spin. Publications are listed on INSPIRE.

    Professor Schuster is also chair of the Particle Physics & Astrophysics department at Stanford’s SLAC National Accelerator Laboratory.

  • Georgios Skiniotis

    Georgios Skiniotis

    Professor of Molecular and Cellular Physiology, of Structural Biology and of Photon Science

    BioThe Skiniotis laboratory seeks to resolve structural and mechanistic questions underlying biological processes that are central to cellular physiology. Our investigations employ primarily cryo-electron microscopy (cryoEM) and 3D reconstruction techniques complemented by biochemistry, biophysics and simulation methods to obtain a dynamic view into the macromolecular complexes carrying out these processes. The main theme in the lab is the structural biology of cell surface receptors that mediate intracellular signaling and communication. Our current main focus is the exploration of the mechanisms responsible for transmembrane signal instigation in cytokine receptors and G protein coupled receptor (GPCR) complexes.

  • Edward I. Solomon

    Edward I. Solomon

    Monroe E. Spaght Professor of Chemistry and Professor of Photon Science

    Current Research and Scholarly InterestsProf. Solomon's work spans physical-inorganic, bioinorganic, and theoretical-inorganic chemistry, focusing on spectroscopic elucidation of the electronic structure of transition metal complexes and its contribution to reactivity. He has advanced our understanding of metal sites involved in electron transfer, copper sites involved in O2 binding, activation and reduction to water, structure/function correlations over non-heme iron enzymes, and correlation of biological to heterogeneous catalysis.

  • Hirohisa A. Tanaka

    Hirohisa A. Tanaka

    Professor of Particle Physics and Astrophysics

    Current Research and Scholarly InterestsParticle physics and astrophysics, neutrino properties, dark matter

  • Sami Gamal-Eldin Tantawi

    Sami Gamal-Eldin Tantawi

    Professor of Particle Physics and Astrophysics
    On Leave from 09/01/2022 To 04/01/2023

    BioFor over a decade I have advocated for dedicated research efforts on the basic physics of room temperature high gradient structures and new initiatives for the associated RF systems. This required demanding multidisciplinary collaboration to harness limited resources. The basic elements of the research needed to be inclusive to address not only the fundamentals of accelerator structures but also the fundamentals of associated technologies such as RF manipulation and novel microwave power sources. These basic research efforts were not bundled with specific developments for an application or a general program. The emerging technologies promise a broad, transformational impact.

    With this underlying philosophy in mind, in 2006 the US High Gradient Research Collaboration for which I am the spokesman was formed. SLAC is the host of this collaboration, which comprises MIT, ANL, University of Maryland and University of Colorado, NRL and a host of SBIR companies. This led to the revitalization of this research area worldwide. The international collaborative effort grew to include KEK in Japan, INFN, Frascati in Italy, the Cockcroft Institute in the UK, and the CLIC team at CERN.

    This effort led to a new understanding of the geometrical effects affecting high gradient operations. The collaborative work led to new advances in understanding the gradient limits of photonic band gap structures. Now we have a new optimization methodology for accelerator structure geometries and ongoing research on alternate and novel materials. These efforts doubled the usable gradient in normal conducting high gradient linacs to more than 100 MV/m, thus revitalizing the spread of the technology to other applications including compact Inverse Compton Scattering gamma-ray sources for national security applications, and compact proton linacs for cancer therapy.

  • Soichi Wakatsuki

    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.

  • William Weis

    William Weis

    William M. Hume Professor in the School of Medicine, Professor of Structural Biology, of Molecular and Cellular Physiology and of Photon Science

    Current Research and Scholarly InterestsOur laboratory studies molecular interactions that underlie the establishment and maintenance of cell and tissue structure. Our principal areas of interest are the architecture and dynamics of intercellular adhesion junctions, signaling pathways that govern cell fate determination, and determinants of cell polarity. Our overall approach is to reconstitute macromolecular assemblies with purified components in order to analyze them using biochemical, biophysical and structural methods.