Special Feature


Method of the Year 2015

Our choice for Method of the Year 2015 is single-particle cryo-electron microscopy. A collection of articles discusses how recent technical advances, especially the development of direct-detection cameras, have enabled this structural biology technique to make impressive leaps in achievable resolution and, in turn, provide new insights about protein function. We also highlight methods to watch in the upcoming years.

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Editorial

Special feature: Method of the Year 2015

Method of the Year 2015 p1

doi:10.1038/nmeth.3730

The end of 'blob-ology': single-particle cryo-electron microscopy (cryo-EM) is now being used to solve macromolecular structures at high resolution.


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News Features

Special feature: Method of the Year 2015

The field that came in from the cold pp19 - 22

Michael Eisenstein

doi:10.1038/nmeth.3698

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.


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Primer

Special feature: Method of the Year 2015

Single-particle cryo-electron microscopy p23

Allison Doerr

doi:10.1038/nmeth.3700

A brief overview of how to solve a macromolecular structure using single-particle cryo-electron microscopy (cryo-EM).


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Historical Commentary

Special feature: Method of the Year 2015

The development of cryo-EM into a mainstream structural biology technique pp24 - 27

Eva Nogales

doi:10.1038/nmeth.3730

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.


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Commentary

Special feature: Method of the Year 2015

How good can cryo-EM become? pp28 - 32

Robert M Glaeser

doi:10.1038/nmeth.3695

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.


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Methods to Watch

Special feature: Method of the Year 2015

Protein labeling in cells p33

Rita Strack

doi:10.1038/nmeth.3702

Better protein-labeling strategies will improve imaging.


Special feature: Method of the Year 2015

Unraveling nuclear architecture p33

Nicole Rusk

doi:10.1038/nmeth.3703

New approaches are needed to see the dynamics of 3D chromatin structure at high resolution and throughput.


Special feature: Method of the Year 2015

Protein structure through time p34

Allison Doerr

doi:10.1038/nmeth.3704

Advances in time-resolved crystallography make it possible to follow ever more rapid protein structural changes.


Special feature: Method of the Year 2015

Precision optogenetics p34

Nina Vogt

doi:10.1038/nmeth.3705

Optogenetic manipulation of neurons at cellular resolution holds promise for the dissection of neural microcircuitry.


Special feature: Method of the Year 2015

Highly multiplexed imaging p35

Rita Strack

doi:10.1038/nmeth.3706

Methods for imaging multiple targets in a single cell are breaking the color barrier.


Special feature: Method of the Year 2015

Deep learning p35

Nicole Rusk

doi:10.1038/nmeth.3707

New computational tools learn complex motifs from large sequence data sets.


Special feature: Method of the Year 2015

Subcellular maps p36

Natalie de Souza

doi:10.1038/nmeth.3708

Methods to systematically map the distribution of proteins in cells are evolving.


Special feature: Method of the Year 2015

Integrated single-cell profiles p36

Tal Nawy

doi:10.1038/nmeth.3709

Integrated molecular profiles of single cells will provide mechanistic insights into gene regulation and heterogeneity.


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