News & Views

A new method for expressing functional RNA molecules in vivo opens a route to easy RNA sample preparation, and establishes a set of tools for studies of RNA structure, interactions and function in vitro and in vivo.

A new mass spectrometry (MS) approach has been developed, allowing combinatorial analysis of histone H3.2 post-translational modifications that may provide the key to unlocking the histone code.

Several new approaches to tag mRNA allow real-time imaging of mRNA dynamics in living bacteria, yeast and human cells.

Enzymatically generated small interfering RNAs are a welcome addition in the tool box of scientists performing large-scale RNAi screens.

Although new super-resolution imaging techniques provide valuable biological insights, some applications, such as determining the organization of neural projections in the brain, are better served by comprehensive imaging of very large samples at lower resolution.

Researchers describe a general and highly efficient approach for incorporating a variety of unnatural amino acids into proteins at desired locations in mammalian cells.

Vectors allowing hydrophilic compounds to gain access to the cell interior are needed to reach new therapeutic targets. Transduction peptides have opened the way to this, but their chemical mimics may be of even greater interest.

Cellular imaging by fluorescence microscopy is becoming simultaneously higher-throughput and more quantitative as researchers develop integrated systems for image acquisition and analysis.

A method of time-resolved two-photon volume imaging with cellular resolution allows for the first time a comprehensive analysis of cortical microcircuits in vivo.

A new maximum likelihood–based algorithm allows cryo-EM structure determination of macromolecular complexes even when conformational heterogeneity is present.

A new method for analyzing membrane protein oligomerization by bioluminescence resonance energy transfer (BRET) suggests that dimerization of G protein–coupled receptors (GPCRs) may not be as prevalent as commonly believed.

Protein-protein interactions are at the heart of the cellular machinery. Direct in-cell visualization of single, endogenous protein interaction pairs now becomes possible.

Two new protein fragment complementation methods expand the toolkit available for the detection of protein interactions in living cells.

A novel atomic force microscopy (AFM) setup allows researchers to image and manipulate unsupported membrane proteins separating two aqueous compartments. This promises to permit new detailed measurements of protein conformational changes and interactions under native-like conditions.

Affinity purification combined with mass spectrometry (AP-MS) is an increasingly important tool for both high-throughput and low-throughput analysis of stable protein complexes in cells. Two groups further expand the capabilities of this experimental approach.

A new twist to a classic technique offers a new way to accurately measure population diversity at the nucleic acid level.

Methods to simultaneously localize the positions of multiple single fluorophores by precisely determining their individual positions are now yielding impressive gains in fluorescence microscopy resolution.

The combination of appropriate labeling and a new imaging software allows researchers to follow the progress of individual HIV particles within infected cells with outstanding precision.

DNA containing a new unnatural base pair may be amplified by PCR and transcribed into RNA, potentially increasing the diversity available from nucleic acids.