Characterisation, crystallisation and preliminary X-ray diffraction analysis of a Fab fragment of a rat monoclonal antibody with very high affinity for the human muscle acetylcholine receptor.

@article{Kontou1996CharacterisationCA,
  title={Characterisation, crystallisation and preliminary X-ray diffraction analysis of a Fab fragment of a rat monoclonal antibody with very high affinity for the human muscle acetylcholine receptor.},
  author={Maria Kontou and E H Vatzaki and Anna Kokla and Keshab R. Acharya and Nikos G. Oikonomakos and Socrates J Tzartos},
  journal={FEBS letters},
  year={1996},
  volume={389 2},
  pages={195-8}
}
The Fab fragment of a rat monoclonal antibody (no. 192) with very high affinity for the main immunogenic region of the human muscle nicotinic acetylcholine receptor (AChR) has been purified, characterised and crystallised using vapour diffusion techniques. Its Kd for human AChR was determined to be 5 X 10(-11) M. Its cross-reactivity pattern suggests that residue alpha23 of the AChR strongly affects its epitope. Crystals suitable for X-ray analysis, obtained by micro- and macroseeding… CONTINUE READING