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Serial Lift-Out creates a series of lamellae from one lift-out volume for cryo-ET, increasing the ease and throughput of cryo-lift-out and enabling the study of molecular anatomy in multicellular systems including C. elegans larvae.

RNA polymerase I is the central enzyme that synthesizes ribosomal RNA in eukaryotic cells, and its regulation underlies cell growth. Here the authors present a high-resolution cryo-EM structure of the Pol I-Rrn3 complex that explains how Rrn3 specifically recognizes Pol I to form an initiation competent complex.

Although the resolution achievable with cryo-EM can now rival crystallography, its application to small protein assemblies remains challenging. Here the authors demonstrate the use of the Volta phase plate for single particle analysis and its potential for the study of small specimens.

Antibody-mediated immune responses rely on antigen recognition by the B cell antigen receptor (BCR) and SLP65 is a key scaffold protein mediating BCR signaling. Here authors show that effective B cell activation requires tripartite phase separation of SLP65, CIN85, and lipid vesicles.

Magnetic nanoparticles are synthesized in a foreign host after gene transfer from magnetotactic bacteria.

The three-dimensional architecture of the cyanobacterium Synechocystis was determined by in situ cryo-electron tomography. The tips of multiple thylakoids merge and contact the plasma membrane, performing a specialized biogenic function.

The large and small subunits of the ribosome are synthesized independently within the nucleolus — a membrane-less compartment within the nucleus — before being exported into the cytoplasm. Here, the authors use in situ cryo-ET to observe ribosome maturation and reveal the native organization of the nucleolus.

Sarcomeres, the building blocks of striated muscles, comprise ordered actomyosin arrays involved in force production. Here, the authors visualize sarcomere organization in neonatal cardiomyocytes with in situ cryo-electron tomography, revealing a reduced order of the thin filaments, their sliding and functional states enabling contraction.

The structure of a complex containing calcitonin gene-related peptide, the human calcitonin gene-related peptide receptor and the G_s heterotrimer, determined using Volta phase-plate cryo-electron microscopy, provides structural insight into the regulation of G-protein-coupled receptors by receptor activity modifying protein 1.

The cryo-electron microscopy structure of the human adenosine A₁ receptor in complex with adenosine and heterotrimeric G_i2 protein provides molecular insights into receptor and G-protein selectivity.

The translocon-associated protein complex (TRAP) is a crucial component of the endoplasmic reticulum protein translocon. Here the authors study native translocon structures from human disease patients and algae cells to determine the molecular organization of the TRAP complex.

Magnetotactic bacteria must assemble magnetosomes into a linear chain that orients the cell along magnetic fields, yet how spiral bacteria with highly curved surfaces accomplish this is unclear. Here, MamY is shown to assemble into linear structures that serve as a scaffold for magnetosomes in magnetotactic spirilla.

Artificial compartments have been expressed in prokaryotes and yeast, but similar capabilities have been missing for mammalian cell engineering. Here the authors use bacterial encapsulins to engineer genetically controlled multifunctional orthogonal compartments in mammalian cells.

While the architecture of vertebrate nuclear pore complexes (NPCs) is well understood, the extent of its evolutionary conservation is still unclear. Here, the authors analyze the in situ architecture of an algal NPC, revealing distinct structural features that provide insights into NPC evolution.

Cryo-EM and X-ray crystallography to determine the mammalian RNA Pol II–DSIF complex structure maps DSIF's polymerase, DNA-template and transcript contacts that facilitate transcription elongation.

The Paf1 complex (Paf1C) is an elongation factor assembly that forms the interface between transcribing Pol II and chromatin factors. Here the authors describe the architecture of Paf1C and its interface with Pol II, and show that Paf1C is globally required for normal mRNA transcription in yeast.

Cryo-electron-microscopy imaging of hibernating ribosomes from Escherichia coli elucidates the molecular composition of these complexes and their mode of assembly, reveals how translation initiation is inhibited, and identifies a role for the ribosomal protein S1 in ribosome inactivation.

The first high-resolution, cryo-electron microscopy structure of mammalian RNA polymerase II, in the form of a transcribing complex comprising DNA template and RNA transcript.

High-resolution structural analysis of macromolecular complexes by cryo-ET requires extremely thin samples. This protocol describes how to prepare thin specimens using FIB milling from frozen cells on grids, which enables direct structural analysis of biomolecules in their native environments, i.e., cells.