Cocaine abuse remains a major public health problem despite ongoing research aimed at developing therapies to counter its harmful effects. Immunopharmacotherapy is one proposed therapy which would block cocaine in the blood stream before it reaches the central nervous system. Cocaine-binding antibodies seem likely candidates for soaking up drugs in the blood stream, but their only binding abilities are not sufficient to withstand high concentrations of the drug. What is needed is a monoclonal antibody with high binding characteristics and sufficient catalytic ability to metabolize cocaine.
Approximately 1,700 scientists visit SSRL annually to conduct experiments in broad disciplines including life sciences, materials, environmental science, and accelerator physics. Science highlights featured here and in our monthly newsletter, Headlines, increase the visibility of user science as well as the important contribution of SSRL in facilitating basic and applied scientific research. Many of these scientific highlights have been included in reports to funding agencies and have been picked up by other media. Users are strongly encouraged to contact us when exciting results are about to be published. We can work with users and the SLAC Office of Communication to develop the story and to communicate user research findings to a much broader audience. Visit SSRL Publications for a list of the hundreds of SSRL-related scientific papers published annually. Contact us to add your most recent publications to this collection.
March 2006
Macromolecular Crystallography
BL9-2
March 2006
Severe acute respiratory syndrome (SARS) emerged as the first severe and readily transmissible new disease of the 21st century. The debilitating pneumonia-like disease is caused by coronavirus, which caused 916 deaths out of about 8,400 reported cases. Scientists from The Scripps Research Institute in California have embarked on an ambitious program to characterize the structure and function of all the proteins built or used by SARS. Taking advantage of advances in robotics and automation at Stanford Synchrotron Radiation Laboratory as well as other new tools, the scientists ultimately hope to rapidly characterize the complete protein sets of emerging disease organisms and then provide structure information to design inhibitors to stop the organisms.
Macromolecular Crystallography
BL1-5, BL11-1, BL11-3
February 2006
SSRL and Stanford scientists, in collaboration with a team from UC Irvine, have gotten the first look into how the metal active center of an enzyme that is largely responsible for fertilizing plants is assembled. This enzyme, which is called nitrogenase, certain bacteria employ to turn nitrogen from the air into a form that plants can use for healthy growth. In contrast to the enzymatic reaction, manufacturing nitrogen fertilizer chemically requires extreme pressures and temperatures and thus huge amounts of energy.
X-ray Absorption Spectroscopy
BL9-3
January 2006
Researchers at SSRL and Stanford have taken a step closer to hydrogen-run cars by adding hydrogen to tiny cylinders made entirely out of carbon. Recent experiments at SSRL and the Advanced Light Source in Berkeley have shown that carbon nanotubes, 50,000 times narrower than a human hair, are a promising material for storing hydrogen safely, efficiently and compactly. To attempt to store hydrogen, the researchers bombarded a film of carbon nanotubes with a hydrogen beam. Then they studied the film with different x-ray spectroscopy techniques to see if any hydrogen atoms had formed chemical bonds with the carbon.
X-ray absorption spectroscopy imaging
December 2005
Research performed at SSRL has provided insight into why lead is so damaging to the healthy development of young children. Scientists from the University of Michigan and Northwestern University used x-ray absorption spectroscopy at SSRL to understand how lead can interfere with proteins that help transform DNA blueprints into working proteins that run the body.
X-ray Absorption Spectroscopy
BL9-3
December 2005
Using x-ray diffraction data collected at SSRL, Scripps researchers Jason Yano, Eric F. Johnson, C. David Stout, and their colleagues have solved the structure of a type of human P450 enzyme called CYP2A6, which is the principal enzyme in the body that degrades nicotine.
Macromolecular Crystallography
BL9-1, BL11-1
November 2005
When a snowball melts, you can tell it has achieved a liquid state when the frigid water drips through your fingers. But if you could follow the melting process, driven by the heat of your hand, from its very first moments - the first trillionth of second, would you be able to point to the exact moment the snowflake crystals disorder into liquid H2O? That's the challenge facing researchers using the Sub-Picosecond Pulse Source (SPPS) to probe the activities of materials on ultrafast timescales. SPPS makes intense x-ray pulses lasting quadrillionths of a second (femtoseconds), enabling researchers to directly monitor the earliest atomic changes during melting with ultrafast x-ray diffraction.
X-ray diffraction
October 2005
Henry VIII's warship, the Mary Rose, wreaked havoc on the French navy for 34 years until she was wrecked in 1545. Salvaged from the sea in 1982, she now rests in the Mary Rose Museum in Portsmouth, England. Pieces of her helm recently traveled to SSRL and the ESRF in Grenoble, France, where intense x-rays pierced the wood to analyze the sulfur and iron within. Led by University of Stockholm Professor Magnus Sandström, researchers had studied another historical treasure, the Swedish warship Vasa, at SSRL in a similar way in 2001.
BL6-2
October 2005
Microtubules, 25 nanometer scale hollow tubules, are critical components in a broad range of functions in eukaryotic cells -- from providing tracks for the transport of cargo to forming the spindle structure for chromosome segregation before cell division. They are used as nanometer scale tracks in neurons for the transport of neurotransmitter precursors and enzymes to synaptic junctions in nerve cell communication.
X-ray scattering
BL4-2
September 2005
X-rays intended to elucidate the structure of biomolecules may actually damage and alter key parts of the molecules. A research team led by a group from Lawrence Berkeley National Laboratory (in collaboration with researchers from Max-Planck-Institut Mülheim, ESRF, SSRL, and TU Berlin and Freie Universität, Berlin) discovered this while investigating the Mn4Ca complex, a site crucial for splitting water into oxygen during photosynthesis.
X-ray Absorption Spectroscopy
BL9-3, BL10-2
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