Single particle macromolecular structure determination via electron microscopy.
Three-dimensional structure determination of macromolecules and macromolecular complexes is an integral part of understanding biological functions. For large protein and macromolecular complexes structure determination is often performed using electron cryomicroscopy where projection images of individual macromolecular complexes are combined to produce a three-dimensional reconstruction. Single particle methods have been devised to perform this structure determination for macromolecular complexes with little or no underlying symmetry. These computational methods generally involve an iterative process of aligning unique views of the macromolecular images followed by determination of the angular components that define those views. In this review, this structure determination process is described with the aim of clarifying a seemingly complex structural method.
Thuman-Commike
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QED Labs, 1190 S. Bascom Ave., Suite 208, San Jose, CA 95128, USA. pam@qedlabs.com
D001435:Bacteriophages / Q000737:chemistry; D020285:Cryoelectron Microscopy; D005583:Fourier Analysis; D007091:Image Processing, Computer-Assisted / Q000379:methods; D021621:Imaging, Three-Dimensional / Q000379:methods; D008854:Microscopy, Electron / Q000379:methods*; D008954:Models, Biological; D008958:Models, Molecular; D008961:Models, Structural; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012269:Ribosomal Proteins / Q000737:chemistry
D012269:Ribosomal Proteins; C040469:ribosomal protein S30