This proposal forms part of a multi-institution Science and Technology Center (STC) proposal to National Science Foundation (NSF). If funded, the program would run for five years (renewable for another five) with twenty-five million dollar total budget (for 5 years) shared between SUNY (lead institution), Stanford, Milwaukee, UCSF, Cornell and ASU. About half the budget is devoted to outreach, technology transfer and education, run by centers at UC Davis and SUNY Buffalo. The research topic concerns the use of the recently-invented X-ray laser for structural biology. Our aim is to use the X-ray laser at SLAC, near Stanford, to obtain movies of molecular machines at work. The director of the STC is Prof E. Lattman at the Hauptman-Woodward institute at SUNY, the Director of Research is Professor Spence at ASU. A pre-proposal submitted in mid 2011 was successful. If funded, funding would start early in 2013. ASU faculty include: Fromme, Doak, Weierstall, Spence and Hogue (Biodesign). The development of hard x-ray, free-electron lasers (XFEL), as exemplified by the linac coherent light source (LCLS) at Stanford, promises a profound revolution in scientific knowledge. Synchrotron x-ray sources have transformed many areas of science over the past 40 years, including crystallography, materials science, high-pressure studies, and x-ray scattering, through their high brilliance, tunability, and pulsed beam structure. The LCLS is a technological leap over synchrotron sources producing X-ray pulses as short as 10 femtoseconds (10-14 seconds) containing up to 1013 photons. This pushes the experimental limit to smaller samples, weaker scatterers and finer time resolution. The beam produces coherent scattering across micrometer-sized objects, enabling whole new imaging modalities previously impossible. The LCLS, and counterparts under construction or planned, provide access to hitherto inaccessible experimental regimes. The STC on X-ray Lasers in Biology will focus its scientific efforts on the use of the FEL to determine structures, and to reveal dynamical behavior through snapshot imaging, of large macromolecular complexes and viruses that cannot easily be studied by other methods. Perhaps they cannot be crystallized (the principal precursor for structural studies); perhaps their action depends on large molecular motions, or perhaps they display structural variability on which biological interactions depend. These structures are crucial to our fundamental understanding of the molecular mechanisms and machines responsible for the biological world around us.
|Effective start/end date||8/1/13 → 9/30/18|
- NSF-OD: Office of Integrative Activities (OIA): $5,764,846.00
x ray sources
x ray scattering
free electron lasers