Abstract

High resolution structures of virus-receptor complexes have been an elusive goal since the first crystal structures of animal viruses were solved about 25 years ago. In part due to the lack of this structural information, the ways in which the receptors interact with their cognate viruses are not well understood at the molecular level even though many viral receptors have now been identified. The recent determination of the crystal structures of a minor group human rhinovirus (HRV2) bound to fragments of its cellular receptor protein offers insights into the peculiarities of the high resolution studies of these complexes. Stable and homogeneous samples of the virus-receptor complexes were required to obtain well diffracting crystals. Data collection and structure determination were performed according to the strategies of virus crystallography.

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