Researchers at Arizona State University’s Biodesign Institute conducted the first systematic study of Holliday junctions—the nexus of two segments of double-stranded DNA—using crystallography techniques performed at the Advanced Light Source, the Argonne Photon Source, and the National Synchrotron Light Source II.
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.
The biopolymer has far-reaching potential from medical therapeutics to replacing synthetic plastics. Armed with a deep understanding of how the enzymes makes acholetin, scientists now have a target for preventing bacterial contamination and the means to produce acholetin for a variety of purposes.
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.