Crystallization of Sendai virus HN protein complexed with monoclonal antibody Fab fragments

The hemagglutinin-neuraminidase (HN) protein of Sendai virus has been isolated from virus particles in a biologically active soluble form after removal by proteolytic digestion of the hydrophobic amino-terminal anchor sequence (S. D. Thompson, W. G. Laver, K. G. Murti, A. Portner, J. Virol., 62, 4653-4660, 1988). The soluble HN exists as both dimers and tetramers, and crystallization trials with each of these forms have so far yielded amorphous material. Dimers complexed with Fab fragments of a monoclonal antibody formed long needle crystals. So far, these are not suitable for X-ray diffraction analysis but the results suggest that HN molecules from paramyxoviruses, even if not crystallizable, may, when complexed with Fab fragments, in some cases yield crystals suitable for X-ray diffraction analysis.