Numerous Biosciences Area personnel are among the 2021 Berkeley Lab Director’s Awards honorees. This annual program recognizes outstanding contributions by employees to all facets of Lab activities. A complete list of winners can be found here. The 10th annual Director’s Awards ceremony will take place on November 18 at noon.
Within each cell of the human body, thousands of molecular machines are at work. They transport nutrients and biochemicals into and out of our cells, build other tiny machines, and even move our cells around. To understand how these molecular machines work, scientists create three-dimensional pictures using electron cryomicroscopy (cryo-EM), catching these machines in different shapes that give insight into their function. Now researchers at Berkeley Lab and their international collaborators who write and distribute the Phenix software suite have developed a new set of computational tools for automated structure determination from cryo-EM data.
Molecular Biophysics and Integrated Bioimaging (MBIB) Division scientists led by Eva Nogales have resolved the 3-D structure of a critical human cellular protein complex involved in DNA transcription and repair at an unprecedented level of resolution. The complex, called transcription factor IIH (TFIIH), unzips the DNA double helix so that genes can be accessed and read. Malfunctions of the complex are associated with premature aging, cancer propensity, and a variety of other defects. One challenge with solving the structure of TFIIH has been that it exists in such minute amounts that it is difficult to produce and purify in large quantities. Moreover, once obtained, it may not form crystals suitable for X-ray diffraction. The researchers used cryo-electron microscopy (cryo-EM), a technique in which purified samples are flash-frozen at ultra cold temperatures, and which works even on very small quantities. “The fact that we resolved this protein structure from human cells makes this even more relevant to disease research,” said Nogales. Basil Greber, a postdoctoral fellow in Nogales’s lab, was first author on the study published in the journal Nature. Computational research scientist Pavel Afonine and MBIB Division Director Paul Adams also contributed to the project. Read more from the Berkeley Lab News Center.
Cryo-electron microscopy is a critical tool used to advance biochemical knowledge. Now Pavel Afonine, research scientist, and Molecular Biophysics and Integrated Bioimaging Division Director Paul Adams have extended cryo-EM’s impact further by developing a new computational algorithm that was instrumental in constructing a 3-D atomic-scale model of bacteriophage P22 for the first time. Read more in the Berkeley Lab News Center.
An international team of scientists is getting closer to discovering how plants split water during photosynthesis and produce nearly all of the oxygen in our atmosphere. Thanks to unprecedented, atomic-scale images of a protein complex found in plants, algae, and cyanobacteria captured by ultrafast X-ray lasers, researchers conducted atomic-level experiments to help delineate the mechanism of this system that also yields the protons and electrons used to reduce carbon dioxide to carbohydrates later in the photosynthesis cycle. The effort to uncover the secrets of this protein complex, photosystem II, was led by Vittal Yachandra and Junko Yano in the Molecular Biophysics & Integrated Bioimaging (MBIB) Division and the team’s findings were published this week in Nature.