Computational protocol: Tau Antibody Structure Reveals a Molecular Switch Defining a Pathological Conformation of the Tau Protein

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Protocol publication

[…] Concentrated Fab C5.2 was mixed with the peptide pS396/pS404 at a 1:10 molar ratio. Crystallization conditions were screened and optimized using the vapor diffusion hanging drop method. Well-diffracted crystals were obtained in a solution containing 25.5% polyethylene glycol 4000, 0.17 M ammonium sulfate and 15% glycerol. X-ray diffraction data were collected at 100 K at a wavelength of 0.979 Å at the Stanford Synchrotron Radiation Lightsource (SSRL) beamline 14–1. The data set to 2.09 Å was processed using the XDS software package and the structure determined by molecular replacement using an initial model with high sequence similarity (Table ). Multiple steps of refinement were carried out in COOT and PHENIX. The final structure analysis was carried out in ICM and figures were generated with Chimera and PyMOL ( The final Rwork and Rfree of the model are 21.8% and 27.0%, respectively, with 97.25% of the residues in the preferred regions and 2.67% in the allowed regions of the Ramachandran plot. […]

Pipeline specifications

Software tools XDS, Coot, PHENIX, PyMOL
Applications Small-angle scattering, Protein structure analysis
Diseases Alzheimer Disease, Neurodegenerative Diseases, Tauopathies