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Volume 10 Issue 2, February 2003

Cryo-EM structures of bacteriophage P22 at 9 å resolution. The overall fold and secondary structure elements of the capsid protein can be visualized in the structures of the procapsid (top) and the mature phage (bottom). Analysis provides insights into changes that occur during bacteriophage maturation. See pages 131–135.

Editorial

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News & Views

  • Real time measurements of conformational switching in single Holliday junctions reinforce the role of the junction in the site selection and branch migration steps of genetic recombination.

    • Mair E.A. Churchill
    News & Views
  • Time-resolved X-ray absorption has been used to investigate the structure of the Zn active site in alcohol dehydrogenase during catalysis. The results support a new mechanistic model for catalysis.

    • James E. Penner-Hahn
    News & Views
  • Because some translation factors mimic the shape of tRNA, they were thought to bind the ribosome in a similar manner. Recent work suggests that this idea of molecular mimicry needs to be reassessed.

    • Ditlev E. Brodersen
    • V. Ramakrishnan
    News & Views
  • Two recent studies show that some ATP-dependent chromatin remodeling complexes are subject to control by a surprising set of regulators — phosphoinositols. These studies extend earlier observations in mammalian cells and suggest that second messengers are regulators of chromatin remodeling.

    • Oliver J. Rando
    • Tian H. Chi
    • Gerald R. Crabtree
    News & Views
  • In vivo selection improves the folding efficiency of the GroELS chaperone toward a specific substrate. Optimizing efficiency, however, comes at the price of narrowed substrate specificity.

    • Annette Erbse
    • David A. Dougan
    • Bernd Bukau
    News & Views
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Meeting Report

  • The CASP5 meeting highlights the evolving role of the initiative: learning from past experience and teaching computers to predict protein structures.

    • Anna Tramontano
    Meeting Report
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