A phage library-derived single-chain Fv fragment in complex with turkey 
egg-white lysozyme: characterization, crystallization and preliminary X-ray 
analysis

Küttner, G.; Keitel, Thomas; Griessmann, E.; Wessner, H.; Scholz, C.; Hoehne, W.

doi:10.1016/S0161-5890(98)00027-3

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A phage library-derived single-chain Fv fragment in complex with turkey egg-white lysozyme: characterization, crystallization and preliminary X-ray analysis

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Keitel, Thomas
Max Planck Research Group Ion Channel Structure (Dean R. Madden), Max Planck Institute for Medical Research, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/S0161589098000273/pdfft?md5=e776266ef5ea1ee84e3f5cbfe70a151c&pid=1-s2.0-S0161589098000273-main.pdf
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Citation

Küttner, G., Keitel, T., Griessmann, E., Wessner, H., Scholz, C., & Hoehne, W. (1998). A phage library-derived single-chain Fv fragment in complex with turkey egg-white lysozyme: characterization, crystallization and preliminary X-ray analysis. Molecular Immunology, 35(3), 189-194. doi:10.1016/S0161-5890(98)00027-3.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-9BAA-4

Abstract

Using phage-display, an anti-turkey egg-white lysozyme single-chain Fv fragment was selected from a naive light chain variable region repertoire in combination with a heavy chain variable region 'mini library' of anti-hen egg-white lysozyme single-domain binders (Ward et al., 1989). Whereas the selected VH domain alone binds somewhat better hen egg-white lysozyme than turkey egg-white lysozyme, but both with comparatively low affinity, the specificity of VH is converted by addition of the VL domain. Thus, the single-chain Fv fragment is more specific for turkey egg-white lysozyme, with markedly increased affinities towards both lysozymes. The complex of single-chain Fv with turkey lysozyme has been crystallized and characterized by preliminary X-ray analysis.