Super-resolution biomolecular crystallography with low-resolution data

Gunnar F. Schröder (), Michael Levitt and Axel T. Brunger ()
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Gunnar F. Schröder: Institut für Strukturbiologie und Biophysik (ISB-3), Forschungszentrum Jülich, 52425 Jülich, Germany
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

Nature, 2010, vol. 464, issue 7292, 1218-1222

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.

Date: 2010
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DOI: 10.1038/nature08892

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