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Crystallization and preliminary X‐ray diffraction studies of complexes between an influenza hemagglutinin and fab fragments of two different monoclonal antibodies
Author(s) -
Gigant Benoît,
Fleury Damien,
Bizebard Thierry,
Skehel John J.,
Knossow Marcel
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340230113
Subject(s) - hemagglutinin (influenza) , monoclonal antibody , crystallization , chemistry , peg ratio , antibody , antigen , virology , crystallography , microbiology and biotechnology , biology , virus , immunology , organic chemistry , finance , economics
Fab fragments from two different monoclonal antibodies (BH151 and HC45) which bind to the same antigenic region of the influenza hemagglutinin were crystallized as complexes with the hemagglutinin. The complexes crystallize in PEG 600, pH 6.0, and PEG 2000, pH 8.5, respectively. Both crystals belong to space group P 321, with very similar unit cell dimensions. © 1995 Wiley‐Liss, Inc.