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Crystallization and preliminary X-ray diffraction analysis of tau protein microtubule-binding motifs in complex with Tau5 and DC25 antibody Fab fragments

The Alzheimer's disease‐associated protein tau is an intrinsically disordered protein with no preferred structure in solution. Under physiological conditions, tau binds to microtubules and regulates their dynamics, whereas during the development of neurodegeneration tau dissociates from microtu...

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Published in:	Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2012-10, Vol.68 (10), p.1181-1185
Main Authors:	Cehlar, Ondrej, Skrabana, Rostislav, Kovac, Andrej, Kovacech, Branislav, Novak, Michal
Format:	Article
Language:	English
Subjects:	Amino Acid Motifs Antibodies, Monoclonal Crystallization Crystallization Communications Crystallography, X-Ray Crystals Deposition Diffraction Fab fragments Fragments Immunoglobulin Fab Fragments - chemistry Immunoglobulin Fab Fragments - immunology intrinsically disordered proteins microtubule binding Microtubules - chemistry Microtubules - metabolism Protein Structure, Tertiary Proteins Synchrotrons tau protein tau Proteins - chemistry tau Proteins - immunology tau Proteins - metabolism X-ray sources X-rays
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creator	Cehlar, Ondrej Skrabana, Rostislav Kovac, Andrej Kovacech, Branislav Novak, Michal
description	The Alzheimer's disease‐associated protein tau is an intrinsically disordered protein with no preferred structure in solution. Under physiological conditions, tau binds to microtubules and regulates their dynamics, whereas during the development of neurodegeneration tau dissociates from microtubules, misfolds and creates highly insoluble deposits. To elucidate the determinants of tau‐protein misfolding, tau peptides from microtubule‐binding motifs were crystallized in complexes with Fab fragments of specific monoclonal antibodies. The crystals diffracted to 1.69 Å resolution and gave complete data sets using a synchrotron X‐ray source. Molecular replacement was used to solve the phase problem.
doi_str_mv	10.1107/S1744309112030382
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subjects	Amino Acid Motifs Antibodies, Monoclonal Crystallization Crystallization Communications Crystallography, X-Ray Crystals Deposition Diffraction Fab fragments Fragments Immunoglobulin Fab Fragments - chemistry Immunoglobulin Fab Fragments - immunology intrinsically disordered proteins microtubule binding Microtubules - chemistry Microtubules - metabolism Protein Structure, Tertiary Proteins Synchrotrons tau protein tau Proteins - chemistry tau Proteins - immunology tau Proteins - metabolism X-ray sources X-rays
title	Crystallization and preliminary X-ray diffraction analysis of tau protein microtubule-binding motifs in complex with Tau5 and DC25 antibody Fab fragments
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