The refinement of the haemagglutinin membrane glycoprotein of influenza virus

Abstract

The crystal structure of the haemagglutinin glycoprotein, a trimer from the membrane of influenza virus, has been refined at 3.0 Å resolution to an R factor of 20.4%. The first 23 cycles were carried out on coordinates of an averaged monomer determined from a non-crystallographically threefold-symmetry-averaged electron density map. The contribution of structure factors to the least-squares equations were determined from non-crystallographically averaged gradient difference and curvature Fourier maps. The refinement was restrained using the Hendrickson & Konnert algorithm. These initial cycles were followed by 25 cycles of refinement with trigonometric evaluation of the derivatives on the complete trimer (208 422 daltons) on a Cray 1/S. Forty-eight water molecules and portions of five N-linked oligosaccharides were identified.

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