Open AccessCrystallization and preliminary X‐ray diffraction analysis of two peptides from Alzheimer PHF in complex with the MN423 antibody Fab fragment
Author(s) -
Skrabana Rostislav,
Cehlar Ondrej,
Flachbartova Zuzana,
Kovac Andrej,
Sevcik Jozef,
Novak Michal
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112033477
Subject(s) - chemistry , crystallography , crystallization , monoclonal antibody , peptide , antibody , x ray crystallography , molecule , biophysics , diffraction , biochemistry , biology , physics , immunology , organic chemistry , optics
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.