Abstract
Without doubt, the most signilicant advance made In this field in recent years has been the determination of the threedimensional structures of a number of antibody Fab fragments complexed with their protein antigens. This has provided a view of the interaction between antibody and antigen at atomic resolution for the first time. The last year has seen the publication of details of the latest of these Fab-antigen complex structures together with a wealth of reviews and discussions of the impli cations of the results obtained so far. In addition, there have been considerable efforts directed towards the crystal structure determination of antibody Fab fragments specilic for a variety of small molecules, short peptides and DNA, and therefore we can confidently expect an enormous increase in the amount of structural data available over the next few years. Furthermore, other physical techniques, and especially nuclear magnetic resonance (Nh@, are now begkming to provide more detailed in formation about antibody-antigen complexes, and since these data are recorded from complexes in solution, they complement the crystallographic results.
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