A PHAGE LIBRARY-DERIVED SINGLE-CHAIN FV FRAGMENT IN COMPLEX WITH TURKEY EGG-WHITE LYSOZYME - CHARACTERIZATION, CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS

Using phage-display, an anti-turkey egg-white lysozyme single-chain Fv fragment was selected from a naive light chain Variable region repert oire in combination with a heavy chain variable region 'mini library' of anti-hen egg-white lysozyme single-domain binders (Ward et al., 198 9). Whereas the selected V-H domain alone binds somewhat better hen eg g-white lysozyme than turkey eggwhite lysozyme, but both with comparat ively low affinity, the specificity of V-H is converted by addition of the V-L domain. Thus, the single-chain Fv fragment is more specific f or turkey egg-white lysozyme, with markedly increased affinities towar ds both lysozymes. The complex of single-chain Fv with turkey lysozyme has been crystallized and characterized by preliminary X-ray analysis . (C) 1998 Elsevier Science Ltd. All rights reserved.