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Single-particle cryo-electron microscopy (cryo-EM) has emerged over the last two decades as a technique capable of studying the structure of challenging systems. The author of this Commentary discusses some of the major historical landmarks in cryo-EM that have led to its present success.
Recent advances in cryo-electron microscopy are enabling researchers to solve protein structures at near-atomic resolutions, expanding the biological applicability of this technique. Michael Eisenstein reports.
Cryo-EM has emerged rapidly as a method for determining high-resolution structures of biological macromolecules. The author of this Commentary discusses just how much better this technology may get and how fast such developments are likely to happen.
This review describes methods for increasing the activity and accuracy of the CRISPR-Cas9 system and discusses approaches for assessing off-target cleavage.
The combination of computational protein design and single-site saturation mutagenesis enables engineering of allosteric transcription factors to respond to new small molecules.
An inverted light-sheet microscope enables imaging of mouse embryos from zygote to blastocyst with minimal photodamage and high resolution for automatic lineage tree reconstruction, allowing new insight into cell fate specification.
RiboTaper quantifies the three-nucleotide periodicity in Ribo-seq data to find translated open reading frames (ORFs). The de novo inferred set of ORFs comprehensively defines the cellular proteome across a wide expression range and comprises few additional translated noncoding regions.
Heterologous TRP channels can be used to stimulate or ablate neurons in response to their chemical or thermal agonists in zebrafish larvae, providing a set of tools orthogonal to optogenetic manipulation.