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Freezing-Activated Covalent Organic Frameworks for Precise Fluorescence Cryo-Imaging of Cancer Tissue

Constraint of accessible chromatins maps regulatory loci involved in maize speciation and domestication

1,4-Azaborine Participation Enables Inaccessible Cycloarene with Unique Photophysical Properties

The translation inhibitors kasugamycin, edeine and GE81112 target distinct steps during 30S initiation complex formation

Abstract During bacterial translation initiation, the 30S ribosomal subunit, initiation factors, and initiator tRNA define the reading frame of the mRNA. This process is inhibited by kasugamycin, edeine and GE81112, however, their mechanisms of action have not been fully elucidated. Here we present cryo-electron microscopy structures of 30S initiation intermediate complexes formed in the presence of kasugamycin, edeine and GE81112 at resolutions of 2.0-2.9 Å. The structures reveal that all three antibiotics bind within the E-site of the 30S and preclude 30S initiation complex formation. While kasugamycin and edeine affect early steps of 30S pre-initiation complex formation, GE81112 stalls pre-initiation complex formation at a further step by allowing start codon recognition, but impeding IF3 departure. Collectively, our work highlights how chemically distinct compounds binding at a conserved site on the 30S can interfere with translation initiation in a unique manner.

Cyano-functionalized polyethylenes from ethylene/acrylamide copolymerization

Rational Design of a Quasi-Metal–Organic Framework by Ligand Engineering for Efficient Biomass Upgrading

Nonlinear dynamics and magneto-elasticity of nanodrums near the phase transition

Activated Corrosion and Recovery in Lead Mixed-Halide Perovskites Revealed by Dynamic Near-Ambient Pressure X-ray Photoelectron Spectroscopy

Highly efficient ionic actuators enabled by sliding ring molecule actuation

Dipolar Carbazole Ammonium for Broadened Electric Field Distribution in High-Performance Perovskite Solar Cells

Author Correction: Ultrafast signatures of merocyanine overcoming steric impedance in crystalline spiropyran

Ring-Expansion Metathesis Polymerization under Confinement

Orbital angular momentum control of strong-field ionization in atoms and molecules

Regiodivergent Alkylation of Pyridines: Alkyllithium Clusters Direct Chemical Reactivity

Electrophysiological signatures underlying variability in human memory consolidation

Optical Spin Hall Effect Pattern Switching in Polariton Condensates in Organic Single-Crystal Microbelts

Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry

Molecularly Woven Polymer Aerogels

Structure and function of the geldanamycin amide synthase from Streptomyces hygroscopicus

Abstract Amide synthases catalyze the formation of macrolactam rings from aniline-containing polyketide-derived seco-acids as found in the important class of ansamycin antibiotics. One of these amide synthases is the geldanamycin amide synthase GdmF, which we recombinantly expressed, purified and studied in detail both functionally as well as structurally. Here we show that purified GdmF catalyzes the amide formation using synthetically derived substrates. The atomic structures of the ligand-free enzyme and in complex with simplified substrates reveal distinct structural features of the substrate binding site and a putative role of the flexible interdomain region for the catalysis reaction.

Integer topological defects offer a methodology to quantify and classify active cell monolayers