Better Structures Through Synergy

TRANSLATING THE RIBOSOME:© 2003 Nature Publishing GroupJoachim Frank and colleagues used cryo-electron microscopy to generate this image of the ribosome bound to release factor RF2 in the presence of a stop codon and a P-site tRNA (left). Then the team overlaid an atomic model of RF2, derived from X-ray data (right; colored orange, purple, red, and green to distinguish domains I, II, III, and IV, respectively). (Reprinted with permission, U.B.S. Rawat et al., Nature, 421:87–90, 2003.)

Written byKaren Heyman
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© 2003 Nature Publishing Group

Joachim Frank and colleagues used cryo-electron microscopy to generate this image of the ribosome bound to release factor RF2 in the presence of a stop codon and a P-site tRNA (left). Then the team overlaid an atomic model of RF2, derived from X-ray data (right; colored orange, purple, red, and green to distinguish domains I, II, III, and IV, respectively). (Reprinted with permission, U.B.S. Rawat et al., Nature, 421:87–90, 2003.)

Biologists have long known that every major structural technique has its limitations. In the past few years many researchers have begun to employ, by virtue of necessity, hybrid approaches to solve questions such as protein assembly. "The overriding message these days is that structural biology is not a single technique," says Peter Wright of the Scripps Research Institute in La Jolla, Calif. "NMR [nuclear magnetic resonance], crystallography, EM [electron microscopy], spectroscopies of various sorts, [and] ...

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