The Zika virus (ZIKV) is a mosquito-borne pathogen recently linked to birth defects in infants. At the ALS, researchers have resolved the structure of a key ZIKV protein to 3.0 Å, an important step toward the rational design of drugs capable of disrupting viral functions and halting the spread of the disease. Read more »
Study Sheds Light on How Bacterial Organelles Assemble
Scientists are providing the clearest view yet of an intact bacterial microcompartment (BMC), revealing the polyhedral structure and assembly of this organelle’s protein shell. Having the full structure can help provide important information in fighting pathogens or bioengineering bacterial organelles for beneficial purposes. Read more »
Protein Complex Shows Promise for Berkelium Separation
Scientists found that the element berkelium breaks form with its heavy-element peers by taking on an extra positive charge when bound to a synthetic organic molecule. This property could help scientists develop better methods for handling and purifying nuclear materials. Read more »
A Systematic Approach to Customizing Cyclic Proteins
Proteins consisting of identical subunits arranged symmetrically around a central axis (cyclic homo-oligomers) play key roles in many biological processes. Researchers have now developed a systematic approach to their design and demonstrated its accuracy using protein crystallography and small-angle x-ray scattering. Read more »
Researchers Gain Insight into Protein Critical to Zika Virus Reproduction
Zika virus is a mosquito-borne infectious disease linked to certain birth defects in infants. Scientists have mapped a key viral protein called NS5, which contains two enzymes: one reduces the body’s ability to mount an immune response against infection and the other helps start the genetic replication process. Read more »
How Berkelium Stands Out in a Heavy Metal Crowd
Using several spectroscopic techniques, scientists found that the element berkelium breaks form with its heavy-element peers by taking on an extra positive charge when bound to a synthetic organic molecule. This property could help scientists develop better methods for handling and purifying nuclear materials. Read more »
How Antidepressants Block Serotonin Transport
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 »
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 »
A New Pathway for Radionuclide Uptake
Scientists have reported a major advance in understanding the biological chemistry of radioactive metals, opening up new avenues of research into strategies for remedial action in the event of possible human exposure to nuclear contaminants. 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 »
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