Researchers led by Berkeley Lab Biosciences’ Cheryl Kerfeld (MBIB), who holds a joint appointment at the MSU-DOE Plant Research Laboratory, have provided the first atomic-level resolution picture of an intact bacterial microcompartment (BMC) shell. The intact shell and component proteins from the saltwater bacterium Haliangium ochraceum were crystallized at Berkeley Lab; X-ray diffraction data were collected at the Lab’s Advanced Light Source (ALS) and at the Stanford Synchrotron Radiation Lightsource. Details of the BMC shell’s structure and composition were published in the journal Science.
A Surprise Just Beneath the Surface in Carbon Dioxide Experiment
Research co-led by Berkeley Lab researchers Junko Yano (MBIB) and Ethan Crumlin at the Advanced Light Source (ALS), with collaborators at Caltech’s Joint Center for Artificial Photosynthesis (JCAP), has revealed a surprising driver of a chemical process to reformulate carbon dioxide into more useful compounds. X-ray experiments coupled with theoretical models showed that oxygen atoms near the surface of a copper sample had a more dramatic effect on the early stages of a reaction with carbon dioxide than earlier theories could account for. This work could help make reactions more efficient in converting carbon dioxide into liquid fuels and other products. Read more in the News Center release.
A Hollow Pyramid Unlocks Principles of Protein Architecture
Researchers at UCLA have designed a hollow, pyramid-shaped protein with a controllable cavity size that may aid the capture and release of smaller compounds. The tools used in this work, including small angle X-ray scattering techniques at the SIBYLS beamline in the Advanced Light Source (ALS), will help analyze and optimize designed-protein assemblies and understand their behavior in solution. Read more in the ALS Science Brief.
Designing Cyclic Oligomers: Greater than the Sum of Their Parts
Cyclic proteins that assemble from multiple identical subunits (homo-oligomers) play key roles in many biological processes, including enzymatic catalysis and function and cell signaling. Researchers in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division worked with University of Washington’s David Baker, who led a team to design in silico and crystallize self-assembling cyclic homo-oligomer proteins.
Three Is Not a Crowd: Designed Metalloprotein Trimer Provides Stable Platform for Further Development
University of Washington (UW) researchers have designed a novel protein with properties that could lead to the generation of new photoactive proteins. This three-fold symmetric, self-assembling protein homotrimer contains a highly stable noncanonical amino acid. Noncanonical amino acids are not found among the 20 encoded amino acids in the body and can contain modifications to allow for new functionality. In this case, this amino acid contains a bipyridine group that chelates metal, thereby introducing new photochemical properties into the protein interface, and nucleating the formation of the homotrimer.
An article published last month in PNAS describes this work from a team of scientists led by David Baker at UW, which included Jose Henrique Pereira, Banumathi Sankaran, and Peter Zwart of the Molecular Biophysics & Integrated Bioimaging Division (MBIB). The MBIB scientists developed the crystal screen that was used to crystallize the novel protein and performed X-ray crystallography on Beamline 8.2.1 in the Berkeley Center for Structural Biology at the Advanced Light Source. Their X-ray crystallographic analysis of the homotrimer showed that the design process had near-atomic-level accuracy, demonstrating that computational protein design together with the utilization of noncanonical amino acids could be used to generate novel protein functions. These methods could be used to develop new therapeutics, biomaterials, and metalloproteins with useful optical or photochemical properties.
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