SLAC + Stanford Collaboration

SLAC + Stanford Collaboration

Stanford University operates SLAC for the U.S. Department of Energy (DOE) Office of Science. We run four joint research centers with Stanford that focus on cosmology and astrophysics, materials and energy science, catalysis, and ultrafast science.

Slideshow Biosciences

MFX Station
Diffraction pattern produced can be analyzed to reveal the 3-D structure of the sample biomolecule.

The Biosciences Division builds on SLAC’s unique strengths in X-ray based research to explore biological function on multiple scales, from individual genes, proteins and enzymes to molecular ecosystems. SLAC’s world-class capabilities in ultrafast and high-throughput macromolecular crystallography, small-angle x-ray scattering, imaging and spectroscopy are optimal for revealing the physical and electronic structures of macromolecules in particular – the cornerstones of biological systems. The Biosciences Division works in close partnership with the Linac Coherent Light Source (LCLS) and the Structural Molecular Biology (SMB) Program at Stanford Synchrotron Radiation Lightsource (SSRL), as well as the Stanford Schools of Medicine, Engineering, and Humanities and Sciences, and the Macromolecular Structure Knowledge Center of ChEM-H, to conduct biological research across many scales of time and space and combine theory, observations, experiments, models and simulations. One such example of the Biosciences Division’s partnership with LCLS, SMB, Stanford University and UCSF is the Macromolecular Femtosecond Crystallography (MFX) station, a new experimental station at LCLS which became operational in summer 2016.

The Bioscience Division’s three high-priority research themes are:

  • Conduct an integrative multiscale pilot project to elucidate macromolecular structure, organization, and function relationships and their impact on biological system function and scaling across hierarchical system boundaries. Our initial focus is on the global nitrogen cycle, in particular ammonia oxidation by ammonia oxidizing archaea (AOA), with specific focus on the structure and function relationship and ecosystem adaptation of key enzymes, such as ammonia monooxygenase and nitrite reductase. The research also includes carbon cycling processes, with an initial target on bacterial CO2 fixing enzymes.
  • Develop a new cryo-electron microscopy/tomography (CryoEM/TM) initiative in close collaboration with Stanford University, which will extend our structural characterization capabilities to the elucidation of atomic resolution structures of protein/nucleic acid complexes, the subcellular and cellular scale structures, and augment the existing X-ray capabilities at SSRL and LCLS. The first of state-of-the-art CryoEM instrument will be installed in Building 6 at SLAC early 2017.
  • Pioneer techniques that enable discovery at subcellular to multicellular scales and their translation to ecosystem scales. Thrusts include programs in super-resolution optical microscopy, Ultrafast Electron Diffraction/Microscopy (UED/UEM) and biocomputation of protein complex structures and dynamics in the context of their subcellular arrangements.