After decades of failed attempts, scientists have solved the structure of a protein domain at the center of several major diseases using Berkeley Center for Structural Biology’s beamline 5.0.2.
A recent study published in Nature Plants used a combination of genetic mutation and X-ray crystallography, conducted at the Berkeley Center for Structural Biology, to reveal structural details of a key enzyme involved in plant signaling.
Researchers at the Scripps Institution of Oceanography in San Diego used the Berkeley Center for Structural Biology’s 8.2.2 beamline at the Advanced Light Source to identify structural details of an enzyme that produces a versatile anti-cancer molecule. By virtue of the its unique, ringed structure the molecule crosses the blood-brain barrier and could be instrumental in fighting difficult-to-access brain cancers.
Viruses have evolved a wide variety of ways to exploit parts of their host cells to avoid detection and to grow. Researchers at the Scripps Research Institute and the Berkeley Center for Structural Biology are learning more about how hepatitis C works to deceive its host cells.
At the cellular level, as a virus invades, its DNA or RNA trigger immune responses in the healthy host cells. How this process is triggered and a better understanding of the specific enzymes involved is still being defined. A collaboration across multiple X-ray facilities, including the Berkeley Center for Structural Biology beamlines at the Advanced Light Source (ALS), compared the enzymes involved in both human and insect immune responses. They used protein crystallography to closely examine the structures, and learned that although overall function is similar, each group of organisms has a slightly different DNA-binding surface and resulting molecular immune response.