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

Maria Kontou, Efstratia H. Vatzaki, Anna Kokla, K. Ravi Acharya, Nikos G. Oikonomakos, Socrates J. Tzartos

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

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 K(d) for human AChR was determined to be 5x10-11 M. Its cross-reactivity pattern suggests that residue α23 of the AChR strongly affects its epitope. Crystals suitable for X-ray analysis, obtained by micro- and macroseeding techniques, belong to the orthorhombic space group C2221 and they diffract to 2.8 Å resolution using synchrotron radiation. The unit cell dimensions are α = 83.4 Å, b = 110.0 Å and c = 212.2 Å and there are two Fab molecules per asymmetric unit.

Original languageEnglish
Pages (from-to)195-198
Number of pages4
JournalFEBS Letters
Volume389
Issue number2
DOIs
Publication statusPublished - 1 Jul 1996

Keywords

  • Acetylcholine receptor
  • Crystallisation
  • Main immunogenic region
  • Monoclonal antibody
  • Myasthenia gravis
  • X-ray crystallography

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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