Journal article

Crystalline monoclonal fab fragment with specificity towards an influenza virus neuraminidase.

PM Colman, KH Gough, GG Lilley, RJ Blagrove, RG Webster, WG Laver

J Mol Biol | Published : 1981


An Fab fragment from a monoclonal antibody (NTS10/1) has been crystallized. The antigen, influenza virus A/Tokyo/3/67 (N2) neuraminidase, is also crystalline and its structure analysis is in progress. The Fab crystals are trigonal, space group P3121 with cell dimensions a = 132·3 A ̊, c = 73·8 A ̊. This crystalline material forms a complex with the neuraminidase with an equilibrium binding constant in excess of 1011m-1. The molecular weight of the complex is 406,000 ± 20,000 indicating that four Fab fragments are attached to each neuraminidase tetramer. The separate crystallization of antigen and Fab fragment opens the way to map, for the first time, the complementary surfaces of an antigen-..

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University of Melbourne Researchers