Two recently licensed vaccines against bacterial meningitis contain a bacterial surface protein antigen known as Factor H binding protein (FHbp). The native form of this protein can have low thermal stability, which limits its potential use as an antigen in vaccines. After engineering a more stable Factor H binding protein antigen, scientists from UC San Francisco Benioff Children’s Hospital Oakland determined the structure of the stabilized vaccine with the help of protein crystallography at the Advanced Light Source (ALS) in the Berkeley Center for Structural Biology (Beamline 5.0.1). Read more in the ALS Science Brief.
The CRISPR/Cas9 bacterial genomic editing system identifies and cleaves complementary target sequences in foreign DNA. CRISPR (clustered regularly interspaced short palindromic repeats)–associated (Cas) protein Cas9 begins its work by RNA-guided DNA unwinding to form an RNA-DNA hybrid and displacing a DNA strand inside the protein. Upon binding, Cas9 reorganizes into an R-loop complex that is necessary for it to perform its function. A recent article published in Science describes work done to uncover the structural basis of Cas9’s function.
Scientists have for the first time reengineered a building block of a geometric nanocompartment that occurs naturally in bacteria. The new design provides an entirely new functionality that greatly expands the potential for these compartments to serve as custom-made chemical factories. The work was led by Cheryl Kerfeld, who holds joint appointments with Berkeley Lab’s Molecular Biophysics and Integrated Bioimaging Division, UC Berkeley and the MSU-DOE Plant Research Laboratory at Michigan State University. Markus Sutter, a senior research associate in Kerfeld’s group at Berkeley Lab, collected the X-ray diffraction data used in this study in the Berkeley Center for Structural Biology at the Advanced Light Source. Read more at the Berkeley Lab News Center.
Synthetic radionuclides, such as the transuranic actinides plutonium, americium, and curium, present severe health threats as contaminants, and understanding the scope of the biochemical interactions involved in actinide uptake into cells is instrumental in managing human contamination. Recently, scientists have reported that an iron-binding protein called siderocalin can also bind and transport actinides into cells, a major advance in understanding the biological chemistry of radioactive metals. The research, which included X-ray crystallographic studies in the Berkeley Center for Structural Biology (Beamlines 5.0.1 and 5.0.2) at the Advanced Light Source (ALS), opens up new avenues of research into strategies for remedial action in the event of possible human exposure to nuclear contaminants. In addition, siderocalin, the protein studied, was selected as “Molecule of the Month” by the Protein Data Bank’s educational portal. Read more in the ALS Science Highlight.
Scientists for the first time have viewed how bacterial proteins self-assemble into thin sheets and begin to form the walls of the outer shell for nano-sized polyhedral compartments that function as specialized factories. Researchers in the Molecular Biophysics & Integrated Bioimaging Division determined the 3-D structure of the basic building block protein from crystallized samples in the Berkeley Center for Structural Biology at the Advanced Light Source. Their findings may eventually help improve drug delivery systems. Read more in the Berkeley Lab News Center.