Cryogenic electron microscopy and single-particle analysis

Annual Review of Biochemistry
Dominika Elmlund, Hans Elmlund

Abstract

About 20 years ago, the first three-dimensional (3D) reconstructions at subnanometer (<10-Å) resolution of an icosahedral virus assembly were obtained by cryogenic electron microscopy (cryo-EM) and single-particle analysis. Since then, thousands of structures have been determined to resolutions ranging from 30 Å to near atomic (<4 Å). Almost overnight, the recent development of direct electron detectors and the attendant improvement in analysis software have advanced the technology considerably. Near-atomic-resolution reconstructions can now be obtained, not only for megadalton macromolecular complexes or highly symmetrical assemblies but also for proteins of only a few hundred kilodaltons. We discuss the developments that led to this breakthrough in high-resolution structure determination by cryo-EM and point to challenges that lie ahead.

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Methods Mentioned

BETA
electron microscopy
electron tomography
X-ray
NMR

Software Mentioned

FREALIGN
RELION
SIMPLE
SPARX
IMAGIC
SPIDER
EMAN
PRIME
XMIPP

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