Malfunctions in the complex protein “machinery” of serotonin transport can result in depression, obsessive-compulsive disorder, aggression, anxiety, and Parkinson’s disease. Now, researchers have obtained x-ray crystallographic structures of the difficult-to-crystallize human serotonin transporter bound to two commonly prescribed antidepressant drug molecules. Read more »
ALS Work Using Protein Crystallography
Protein crystallography is used for determining the molecular structure of proteins. Crystallized protein molecules cause a beam of incident x-rays to scatter in many directions, with constructive and destructive interference generating a diffraction pattern. By analyzing these patterns, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal and thus determine the protein's structure.
Understanding the Key to Henipavirus Infection
The Hendra virus was the first member of the genus Henipavirus, an emergent group of viruses with a high mortality rate. Knowledge of the protein structure that mediates Hendra entry into host cells could enable the design of antigens with improved immunogenic response. Read more »
Reducing Plant Lignin for Cheaper Biofuels
Scientists have identified and validated a novel approach to reducing lignin in plants by tweaking a key lignin enzyme. Their technique could help lower the cost of converting biomass into carbon-neutral fuels to power cars and other sustainably developed bio-products. Read more »
Shutting Out Ebola and Other Viruses
Researchers have used protein crystallography at the ALS to understand how a drug molecule that has shown some efficacy against Ebola in mice inactivates a membrane protein, called TPC1, used by viruses to infect host cells. Read more »
Exploring the Repeat-Protein Universe
Researchers have published a landmark study that used both crystallography and SAXS to validate computationally designed structures of novel proteins with repeated motifs. The results show that the protein-folding universe is far larger than realized, opening up a wide array of new possibilities for biomolecular engineering. Read more »
Improving Anti-Influenza Medications
Protein crystallography at ALS Beamline 8.3.1 helped scientists understand the M2 proton-channel structure from the influenza A virus, an understanding that is needed to design better anti-influenza medications. Read more »
Improving Meningococcal Vaccines
Scientists have found a way to improve the stability of an essential antigenic protein to develop vaccines with higher efficacy for prevention of bacterial meningitis. Read more »
Foreign DNA Capture during CRISPR–Cas Adaptive Immunity
Using macromolecular crystallography at Beamline 8.3.1 at the ALS, Berkeley researchers discovered how CRISPR/Cas captures foreign DNA for the bacterial immune system. Read more »
Binding Behavior of Dopamine Transporter Key to Understanding Chemical Reactions in the Brain
Scientists working at the ALS recently solved the crystallographic structures of several amine transporters in an effort to better understand why the human brain responds to chemicals like dopamine and serotonin. What they found will help in the design of drugs to treat many neurological diseases, and may also lead to a better understanding of how addiction to abused drugs such as cocaine can be managed. Read more »
SIBYLS Beamline Builds on Nobel Research
Often the full impact of a scientific discovery takes decades to realize, during which the research is developed further and adopted by other scientists. Such was the case for the work of biochemist Paul Modrich, one of three recipients of this year’s Nobel Prize in Chemistry. Berkeley Lab’s Advanced Light Source was a core resource Modrich used to build on his earlier work. Read more »