CryoEM at IUCrJ: a new era

Abstract

In this overview, we briefly outline recent advances in electron cryomicroscopy (cryoEM) and explain why the journal IUCrJ, published by the International Union of Crystallography, could provide a natural home for publications covering many present and future developments in the cryoEM field.

Keywords: cryoEM; electron cryomicroscopy; electron tomography; overview; single particle.

Figure 1

Growth in number of cryoEM structures deposited at the Electron Microscopy Data Bank since 2002 (taken from the PDB website: http://pdbe.org/emstats). There is exponential growth at all resolution ranges, and a dramatic increase in the number of structures with resolutions better than 4 Å. Earlier studies that represent landmarks in the development of single-particle cryoEM were the hepatitis B capsid determined at 7.4 Å resolution (Böttcher et al., 1997; Conway et al., 1997 ▸) and the E.coli 70S ribosome at 11.5 Å resolution (Gabashvili et al., 2000 ▸).

Figure 2

Selected examples of structures with sizes below 500 kDa. (a) TRPV1 temperature-sensing channel also called the capsaicin receptor (Liao et al., 2013 ▸) at 3.4 Å resolution, (b) γ-secretase at 3.4 Å resolution (Bai et al., 2015 ▸) and (c) β-galactosidase at 2.2 Å resolution (Bartesaghi et al., 2015 ▸). Not on same scale.

Figure 3

Examples of selected medium-sized membrane protein structures. (a) Yeast V-type ATPase at 7 Å resolution (Zhao et al., 2015 ▸), (b) mitochondrial Complex I (Vinothkumar et al., 2014 ▸) at 5 Å resolution, and (c) the anthrax protective antigen pore at 2.9 Å resolution (Jiang et al., 2015 ▸). Scale bar is 25 Å.

Figure 4

Examples of some large structures. (a) Human rotavirus (Grant & Grigorieff, 2015 ▸), (b) brome mosaic virus (Wang et al., 2014 ▸) and (c) TMV (Fromm et al., 2015 ▸), at resolutions of 2.6 Å, 3.8 Å and 3.4 Å, respectively. Not on same scale.