Complementing crystallography: the role of cryo-electron microscopy in structural biology.
Dramatic improvements in experimental methods and computational techniques have revolutionized three-dimensional image reconstruction from electron micrographs (EM) of vitrified samples. Recent results include the first determination of a protein fold (for the core protein of the hepatitis B virus) by non-crystalline imaging techniques. These developments have generated interest within the crystallographic community and have led to a re-evaluation of the technique, particularly amongst those working in the field of virus structure or struggling with the phasing of large macromolecular assemblies. A simple discussion of the techniques of EM image reconstruction and its advantages and problems in terms familiar to crystallographers will hopefully allow an appreciation of the essential complementarity of the two techniques and the practical potentials for phasing applications.
Grimes
J M
JM
Structural Biology Division, The Wellcome Trust Center for Human Genetics, Roosevelt Drive, Headington, Oxford OX3 7BN, England. jonathan@strubi.ox.ac.uk
Fuller
S D
SD
Stuart
D I
DI
D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D006515:Hepatitis B virus / Q000648:ultrastructure; D007091:Image Processing, Computer-Assisted; D012270:Ribosomes / Q000737:chemistry / Q000648:ultrastructure; D012542:Scattering, Radiation; D012672:Semliki forest virus / Q000648:ultrastructure; D014758:Viral Core Proteins / Q000737:chemistry / Q000648:ultrastructure
D014758:Viral Core Proteins