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

$48.00 plus tax (Refund Policy)

Download / Buy Article:

Abstract:

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.

Document Type: Research Article

DOI: http://dx.doi.org/10.1107/S1744309112030382

Publication date: October 1, 2012

Related content

Tools

Favourites

Share Content

Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
X
Cookie Policy
ingentaconnect 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