International Tables for Crystallography
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Four-dimensional cryo-electron microscopy at quasi-atomic resolution: IMAGIC 4D International Tables for Crystallography (2012). Vol. F, ch. 19.9, pp. 624-628 [ doi:10.1107/97809553602060000875 ] Abstract The traditional tools of the structural biologist seeking to understand macromolecules and their complexes are X-ray crystallography and NMR spectroscopy. Single-particle cryo-electron microscopy (cryo-EM) has established itself as a new structural-biology technique over the last 15 years. Spectacular insights into the functioning of macromolecular complexes have been achieved especially from combining cryo-EM with the earlier approaches. The resolution levels achieved improved over the last decade from ∼10 Å to sometimes better than ∼4 Å, meaning that a de novo structure determination based on single-particle cryo-EM studies alone is now feasible. More challenging is the new perspective that cryo-EM brings: sorting heterogeneous populations of molecules into individual three-dimensional conformers resulting in sequences of related three-dimensional structures, or in short `4D cryo-EM'. Thanks to these developments, single-particle cryo-EM has become the technique of choice for shedding light on the functioning of many a complex biological system. The design of the software instrumentation for 4D cryo-EM is crucial. In this chapter we elaborate on organization issues for single-particle cryo-EM software, as exemplified by recent developments in the IMAGIC 4D software system. |
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About International Tables for Crystallography
International Tables for Crystallography is the definitive resource and reference work for crystallography. The multi-volume series comprises articles and tables of data relevant to crystallographic research and to applications of crystallographic methods in all sciences concerned with the structure and properties of materials.