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Cryogenic electron microscopy reveals how dCas12f with σ^E recruits RNAP to targeted DNA, initiating transcription at a fixed downstream distance, bypassing canonical −35 recognition and stabilizing the −10 element in an unusual manner.

Specialized σ factors interact with nuclease-dead, CRISPR–Cas12f proteins to form potent, RNA-guided gene activation systems that function independently of fixed promoter motifs.

The anaphase-promoting complex/cyclosome (APC/C) is a large E3 ligase that mediates ubiquitin-dependent proteolysis of cell cycle regulatory proteins; here the complete secondary structure architecture of human APC/C complexed with its coactivator CDH1 and substrate HSL1 is determined at 7.4 Å resolution, revealing allosteric changes induced by the coactivator that enhance affinity for UBCH10–ubiqutin.

A high-resolution structure of a complex between the anaphase-promoting complex (APC/C) and the mitotic checkpoint complex (MCC) reveals how MCC interacts with and represses APC/C by obstructing substrate recognition and suppressing E3 ligase activity.

A cryo-electron microscopy determination of the atomic structures of anaphase-promoting complex (APC/C)–coactivator complexes with either Emi1 or a UbcH10–ubiquitin conjugate.

Here the authors describes a high-resolution cryo-EM structure of the anaphase-promoting complex (APC/C) revealing insights into regulation of its activity and identifying a zinc-binding site in the APC2 subunit.

Here, the authors synthesize a variety of ultra-thin III–V single crystals, ranging from ultra-narrow to wide bandgap semiconductors, through enhancing the interfacial interaction between the III–V crystals and the growth substrates.

The ultrathin oxide nanosheets obtained through previous approaches usually exhibit amorphism or polycrystallinity, which limit their properties towards electronic devices. Here, the authors synthesize ultrathin antimony oxide single crystals with high dielectric constant (~100) and large breakdown voltage (~5.7 GV m⁻¹).

Mukherjee et al. report that AcrIF24 is an Acr-Aca fusion protein that inhibits the Csy complex and suppresses transcription from the acrIF23–acrIF24 promoter, and they present cryo-EM structures to reveal the mechanism for both roles of AcrIF24.

The eight-subunit augmin complex is required to nucleate branching microtubules and create a robust mitotic spindle during cell division. Here, the authors use cryo-EM, crosslinking mass spectrometry, and computational tools to build a structural model of the human augmin complex.

The cryo-EM structures of Cas12g in complex with sgRNA in the absence and presence of target RNA reveal that the duplex formed by target RNA and crRNA binds to a central channel of Cas12g, inducing its conformational change and activation.

Cryo-EM structures of Cas12i in multiple functional states provide insights that might facilitate the manipulation of this type V CRISPR-Cas endonuclease for genome editing applications.

DOCK2 is a guanine nucleotide exchange factor (GEF) that activates RHO GTPases and interacts with ELMO1, which stimulates its GEF activity. Here, the authors provide mechanistic insights into how ELMO1 regulates DOCK2 activity by determining the structure of the DOCK2–ELMO1 binary complex representing the closed, auto-inhibited state and the DOCK2−ELMO1−RAC1 ternary complex structure, where DOCK2−ELMO1 adopts an open, active conformation.

Cryo-EM structures of complexes between GRK1 and rhodopsin shed light on how a small number of GRKs can selectively recognize and be activated by hundreds of different G-protein-coupled receptors.

Phosphorylation of the anaphase-promoting complex (APC/C) allows for its control by the co-activator Cdc20; a mechanism that has relevance to understanding the control of other large multimeric complexes by phosphorylation.

Cryo-EM analyses provide a near-atomic view of the C. elegans securin–separase complex, with insights into the mechanism by which securin inhibits separase's protease activity.

OAT1 has a fundamental role in the kidney by facilitating the urinary excretion of various drugs and endogenous metabolites. Two studies now present high-resolution structures of OAT1 using cryo-EM, elucidating its intricate polyspecific transport capabilities and paving the way for structure-based drug research and development.

Structural analysis demonstrates how TRIP13 and p31^comet disassemble the mitotic checkpoint complex.

Cryo-electron microscopy structures of the Saccharomyces cerevisiae inner kinetochore complex provide insights into the interdependencies of constituent subcomplexes and the mechanism of centromeric nucleosome recognition.