Crystallization,preliminary X-ray diffraction study,and crystal packing of a complex between anti-Hen lysozyme antibody F9.13.7 and Guinea-fowl lysozyme |
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Authors: | Julien Lescar Marie-Madeleine Riottot Hlne Souchon Vronique Chitarra Graham A Bentley Jorge Navaza Pedro M Alzari Roberto J Poljak |
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Institution: | Julien Lescar,Marie-Madeleine Riottot,Hélène Souchon,Véronique Chitarra,Graham A. Bentley,Jorge Navaza,Pedro M. Alzari,Roberto J. Poljak |
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Abstract: | The complex formed between the Fab fragment of a murine monoclonal anti-hen egg lysozyme antibody F9.13.7 and the het-erologous antigen Guinea-fowl egg lysozyme has been crystallized by the hanging drop technique. The crystals, which diffract X-rays to 3 Å resolution, belong to the monoclinic space group P21, with a = 83.7 Å, b = 195.5 Å, c = 50.2 Å, β = 108.5° and have two molecules of the complex in the asymmetric unit The three-dimensional structure has been determined from a preliminary data set to 4 Å using molecular replacement techniques. The lysozyme–Fab complexes are arranged with their long molecular axes approximately parallel to the crystallo-graphic unique axis. Fab F9.13.7 binds an anti-genie determinant that partially overlaps the epitope recognized by antilysozyme antibody HyHEL10. © 1993 Wiley-Liss, Inc. |
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Keywords: | crystallization antilysozyme system epitope antigen– antibody complex cross-reactivity |
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