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Nature Research congratulates the awardees of the 2017 Nobel Prize in Chemistry - Jacques Dubochet, Joachim Frank and Richard Henderson. Their pioneering work on the use of cryo-electron microscopy to solve high-resolution structures of biomolecules has provided unprecedented insights into the complexity of life. Here, we present a Collection of Research, Methods, Reviews and Comment pieces from Nature Research to celebrate the award.
The combination of a direct electron-detection camera that can count individual electrons and an algorithm for correcting for beam-induced motion in cryo-EM will facilitate determination of three-dimensional structures of smaller, lower-symmetry macromolecular complexes to higher resolution than previously possible.
Using a peptide toxin and small vanilloid agonists as pharmacological probes, high-resolution electron cryo-microscopy structures of rat TRPV1–ligand complexes are solved; these structures highlight conformational differences between TRP and voltage-gated ion channels in their active states, and suggest a dual gating mechanism that may account for the ability of members of the TRP channel superfamily to integrate diverse physiological signals.
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.
A 3.7 Å resolution structure for the yeast U4/U6.U5 tri-snRNP, a complex involved in splicing, allows a better appreciation of the architecture of the tri-snRNP, and offers new functional insights into the activation of the spliceosome and the assembly of the catalytic core.
A cryo-electron microscopy structure of the DNA damage repair protein 53BP1 bound to a nucleosome illuminates the way 53BP1 recognizes two types of histone modifications (a methyl group and a ubiquitin moiety), and provides insight into the highly specified recognition and recruitment of 53BP1 to modified chromatin.
The cryo-electron microscopy structures of yeast initiation complexes containing the transcription factors TBP, TFIIA, TFIIB, TFIIE, and TFIIF and containing either closed or open promoter DNA are reported, providing mechanistic insights into DNA opening and template-strand loading.
Cryo-electron microscopy structural models of the human pre-initiation complex at all major steps of transcription initiation at near atomic-level resolution are presented, providing new mechanistic insights into the processes of promoter melting and transcription-bubble formation, as well as an almost complete proposed structural model of all of the pre-initiation complex components and their interactions with DNA.
Volta phase-plate cryo-electron microscopy reveals the structure of the full-length calcitonin receptor in complex with its peptide ligand and Gαsβγ.
Single particle cryo-EM is commonly used for the structure determination of large complexes. Here, the authors present the 3.2 Å resolution cryo-EM structure of human haemoglobin, which has a molecular weight of 64 kDa.
Using single-particle electron cryomicroscopy, several structures are reported which illuminate the mechanisms of action of the ATPase NSF that disassembles the SNARE complex into individual protein components.
Electron cryomicroscopy reveals the three-dimensional structure of F-actin at a resolution of 3.7 Ă… in complex with tropomyosin at a resolution of 6.5 Ă…; the stabilizing interactions and the effects of disease-causing mutants are also investigated.
Respirasomes are supercomplexes of mitochondrial electron transport chain complexes that are responsible for cellular respiration and energy production; cryo-electron microscopy structures of mammalian (sheep) respirasomes are presented.
A cryo-EM structure of the human 26S proteasome in a resting state at an average resolution of 3.5 Ă… reveals details in the interactions between subunits. An additional structure of the proteasome with USP14 bound suggests a mechanism for its activation.
Combined kinetic and cryo-EM analysis of the R197A mutant of GroEL provides insight into the allosteric switching of GroEL, which is at the heart of the chaperonin mechanism.
Using electron cryomicroscopy, the structure of the rabbit RyR1 calcium channel is determined at 6.1 Ă… resolution in the closed state and 8.5 Ă… in the open state, revealing how calcium binding to the EF-hand of RyR1 regulates channel opening and facilitates calcium-induced calcium release.
Using electron cryomicroscopy, the structure of the closed-state rabbit ryanodine receptor RyR1 in complex with its modulator FKBP12 is solved at 3.8 Ă…; in addition to determining structural details of the ion-conducting channel domain, three previously uncharacterized domains help to reveal a molecular scaffold that allows long-range allosteric regulation of channel activities.
In plants, photosystem II forms supercomplexes of core and light-harvesting complexes. Cryo-electron microscopy and single-particle analysis provides a 3D structure of the supercomplex from Arabidopsis at 5.3 Ă… resolution.