With data obtained at the ALS, researchers gained insight into how an enzyme orchestrates the synthesis of a pectin polymer that imparts strength and flexibility to plant cell walls. The work could lead to improved biofuel production and guide the design of polymers with tailored functionalities for industrial or biomedical applications. Read more »
ALS Work Using Protein Crystallography
Protein crystallography is used for determining the molecular structure of proteins. Crystallized protein molecules cause a beam of incident x-rays to scatter in many directions, with constructive and destructive interference generating a diffraction pattern. By analyzing these patterns, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal and thus determine the protein's structure.
Gemini Beamline 2.0.1 Banks Its First Protein Structure
A protein structure obtained from ALS Beamline 2.0.1 (“Gemini”) has recently been published in the literature and deposited into the Protein Data Bank (PDB)—two significant firsts for this beamline. The structure helped provide new insights into the molecular mechanisms involved in triggering certain inflammatory diseases. Read more »
Chatbot-Style AI Designs Novel Functional Protein
Researchers used an artificial intelligence (AI) algorithm, similar to those used in natural-language (“chatbot”) models, to design a functional protein that was then structurally validated at the ALS. The work could speed the development of novel proteins for almost anything from therapeutics to degrading plastic. Read more »
Uncompetitive, adduct-forming SARM1 inhibitors are neuroprotective in preclinical models of nerve injury and disease
Researchers describe potent small-molecule inhibitors that are neuroprotective in preclinical models of nerve injury and disease. The cover depicts the destruction of an axon by the enzyme SARM1, shown disproportionately large to convey its catastrophic role in driving degeneration once it is activated upon injury. Read more »
Protein Assemblies Show Surprising Variability
Protein-structure studies performed in part at the ALS helped researchers discover that the protein assemblies in a key carbon-cycling enzyme can rearrange with surprising ease. The findings raise the prospect of genetically tuning the protein in agricultural plant species to produce more productive and resource-efficient crops. Read more »
Chemical acylation of an acquired serine suppresses oncogenic signaling of K-Ras(G12S)
Small-molecule targeting of particular KRAS mutations offer promise for cancer therapy. The cover depicts a small-molecule ligand (red) inhibiting the oncogenic mutant protein K-Ras(G12S) (cyan) by forming a covalent ester adduct at the mutant serine. Read more »
An Expanded Set of DNA Building Blocks for 3D Lattices
Researchers studied 36 DNA-based molecular junctions and discovered factors that yield superior self-assembled 3D lattice structures. The work expands the set of building blocks for lattices that can scaffold molecules into regular arrays, from proteins for structure studies to nanoparticles for nano-antennas and single-particle sensors. Read more »
Protein Structures Aren’t Set in Stone
A group of researchers studying the world’s most abundant protein, an enzyme involved in photosynthesis called rubisco, showed how evolution can lead to a surprising diversity of molecular assemblies that all accomplish the same task. The findings reveal the possibility that many of the proteins we thought we knew actually exist in other, unknown shapes. Read more »
Deep-Learning AI Program Accurately Predicts Key Rotavirus Protein Fold
Rotaviruses are the major causative agents of gastroenteritis worldwide. Attempts to design vaccines are complicated by the rotaviruses’ enormous genetic and immunological diversity. At the ALS, researchers validated the novel structure of a key rotavirus protein, predicted using AlphaFold2, a deep-learning artificial-intelligence program. Read more »
Molecular Switch Triggers Changes in Plant Structure
Using x-ray crystallography, biochemistry, and plant genetics, researchers identified a molecular switch that triggers modifications to plant structure in response to environmental conditions. A greater understanding of this adaptive process will help scientists optimize plants for efficient nutrient uptake and resistance to parasitic species. Read more »
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