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Super-resolution biomolecular crystallography with low-resolution data

Author

Listed:
  • Gunnar F. Schröder

    (Institut für Strukturbiologie und Biophysik (ISB-3), Forschungszentrum Jülich, 52425 Jülich, Germany
    Stanford School of Medicine, D100 Fairchild Building, 299 West Campus Drive, Stanford, California 94305, USA)

  • Michael Levitt

    (Stanford School of Medicine, D100 Fairchild Building, 299 West Campus Drive, Stanford, California 94305, USA)

  • Axel T. Brunger

    (Stanford School of Medicine, D100 Fairchild Building, 299 West Campus Drive, Stanford, California 94305, USA
    Howard Hughes Medical Institute,
    Department of Molecular and Cellular Physiology,
    Department of Neurology and Neurological Sciences,)

Abstract

Making more of X-ray crystallography X-ray crystallography has become the most common method used by structural biologists to obtain three-dimensional structures of proteins and protein–protein complexes. However, crystals of large macromolecular complexes often diffract only weakly — yielding a resolution of less than about 4 Å — so it is important to develop new methods that work at such low resolution. Here, the authors show that information from comparative modelling can be combined in a statistically controlled fashion with the observed diffraction data in order to achieve a structure from low-resolution diffraction data that has a similar quality as a high-resolution structure.

Suggested Citation

  • Gunnar F. Schröder & Michael Levitt & Axel T. Brunger, 2010. "Super-resolution biomolecular crystallography with low-resolution data," Nature, Nature, vol. 464(7292), pages 1218-1222, April.
    • Handle: RePEc:nat:nature:v:464:y:2010:i:7292:d:10.1038_nature08892
    DOI: 10.1038/nature08892
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