Advances in cryogenic electron microscopy have enabled an international team of experts to visualize the structure of a cyanobacterial phycobilisome with nearly atomic resolution. The work, a collaboration among researchers at Michigan State University, UC Berkeley, Berkeley Lab, and the University of South Bohemia in the Czech Republic, was published in Nature. Knowing the position of different proteins and pigments helps scientist better understand this natural process and can inspire future applications in areas such as renewable energy and environmental remediation.
Two from Biosciences Named AAAS Fellows
Two scientists from the Biosciences Area, Cheryl Kerfeld and David Schaffer, have been named Fellows of the American Association for the Advancement of Science (AAAS). They join fellow Lab scientists Rebecca Abergel in the Chemical Sciences Division, Roland Burgmann and Michael Manga in the Earth and Environmental Sciences Area Energy Geosciences Division, and Natalie Roe, Director of the Physics Division, in receiving the distinction of Fellow this year for “their scientifically or socially distinguished efforts to advance science or its applications.”
X-ray Footprinting Reveals Molecular Basis of Orange Carotenoid Protein Photoprotection
Researchers at Berkeley Lab and Michigan State University (MSU), led by Corie Ralston and Cheryl Kerfeld, performed X-ray footprinting mass spectrometry (XFMS) experiments at the Advanced Light Source (ALS) beamline 5.3.1, which revealed new mechanistic details of the key events in orange carotenoid protein (OCP) photoprotection. XFMS is ideally suited to probing conformational dynamics at the single residue level, providing both a spatial and temporal view of site-specific changes in the OCP and its interaction with the fluorescence recovery protein (FRP). The experiments showed that FRP provides an extended binding region that holds the OCP together and forces proximity of the two domains that accelerate relaxation of OCP to its native state.
A Synthetic Nanofactory Inspired by Nature
Researchers at Berkeley Lab and Michigan State University (MSU), led by Cheryl Kerfeld, have created a genetically engineered bacterial microcompartment (BMC) shell based on natural structures and the principles of protein evolution. The new shell is smaller and simpler, made of only a single designed protein (natural BMCs are made of up to three), making it easier to work with in the lab.
First Look at New Light Absorbing Protein
The Helical Carotenoid Protein 2 (HCP2) protein is an ancestor of proteins that are known to protect against damage caused by excess light exposure. Researchers in the laboratory of Cheryl Kerfeld, guest faculty in the Environmental Genomics & Systems Biology (EGSB) Division, are the first to structurally and biophysically analyze a protein from the HCP family. This HCP protein family was discovered recently by Kerfeld and the members of her lab, who are based in EGSB and at Michigan State University (MSU). To solve the molecular structure of HCP2, X-ray diffraction was measured at beam line 5.0.2 in the Berkeley Center for Structural Biology of the Advanced Light Source (ALS). The structure was refined using Phenix, a software suite for automated determination of molecular structures developed under the direction of Paul Adams, Molecular Biophysics and Integrated Bioimaging Division Director. Read more in the MSU-DOE Plant Research Laboratory news story.
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