Skip to main content

Crystallization and preliminary X‐ray diffraction analysis of two peptides from Alzheimer PHF in complex with the MN423 antibody Fab fragment

Buy Article:

$51.00 plus tax (Refund Policy)


The major constituent of the Alzheimer's disease paired helical filaments (PHF) core is the intrinsically disordered protein (IDP) tau. Globular binding partners, e.g. monoclonal antibodies, can stabilize the fold of disordered tau in complexes. A previously published structure of a proteolytically generated tau fragment in a complex with the PHF‐specific monoclonal antibody MN423 revealed a turn‐like structure of the PHF core C‐terminus [Sevcik et al. (2007). FEBS Lett. 581, 5872–5878]. To examine the structures of longer better‐defined PHF segments, crystals of the MN423 Fab fragment were grown in the presence of two synthetic peptides derived from the PHF core C‐terminus. For each, X‐ray diffraction data were collected at 100 K at a synchrotron source and initial phases were obtained by molecular replacement.

Document Type: Research Article


Publication date: 2012-10-01

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more