Forty years in cryoEM of membrane proteins

In a surprisingly short time, electron cryo-microscopy (cryoEM) has developed from a niche technique in structural biology to a mainstream method practiced in a rapidly growing number of laboratories around the world. From its beginnings about 40 years ago, cryoEM has had a major impact on the study of membrane proteins, in particular the energy-converting systems from bacterial, mitochondrial and chloroplast membranes. Early work on two-dimensional crystals attained resolutions similar to 3.5 angstrom, but at present, single-particle cryoEM delivers much more detailed structures without crystals. Electron cryo-tomography of membranes and membrane-associated proteins adds valuable context, usually at lower resolution. The review ends with a brief outlook on future prospects.

Automated summary

In a surprisingly short time, cryoEM has become a mainstream method in structural biology, impacting the study of membrane proteins and providing detailed structures without crystals. Single-particle cryoEM provides more detailed information, while cryo-tomography offers valuable context.