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Microcrystal electron diffraction (MicroED) is an electron cryo-microscopy (cryo-EM) technique able to produce high-resolution protein structures from nanocrystalline and microcrystalline material. Employing smaller crystals can improve ligand soaking to reveal new protein-ligand complexes with future potentials in drug discovery. See Clark et al.
Image: Jason Drees and Brent Nannenga, Arizona State University; Tamir Gonen, University of California, Los Angeles. Cover design: Carl Conway.
Rapidly alternating the polarity of electrodes offers a new opportunity for synthetic chemists to obtain selective reaction outcomes in organic electrosynthesis.
This Review establishes a unifying structure–property relationship among chemical composition, centrosymmetry breaking, lattice anharmonicity, ferroelectricity, dielectric screening and the Rashba effect in metal halide perovskites from the perspective of stereochemical expression of ns2 electron pairs on group IV metal cations.
Microcrystal electron diffraction (MicroED) can determine the structure of proteins from crystals that are orders of magnitude smaller than those used by X-ray methods. Here, the application of MicroED to protein–ligand complexes is reviewed.
Reversible addition–fragmentation chain-transfer (RAFT) polymerization and atom transfer radical polymerization (ATRP) are evaluated in terms of their mechanistic strengths and weaknesses, versatility and latest synthetic advances.
We propose that life originated in spontaneously formed catalytic lipid micelles. Accumulating experimental evidence shows that such micelles undergo compositional autocatalytic reproduction. Lipid-first constitutes a parsimonious alternative to the RNA-first scenario.