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Crystallization and preliminary X-ray diffraction analysis of the Fab portion of the Alzheimer's disease immunotherapy candidate bapineuzumab complexed with amyloid-β

Acta Crystallogr F Struct Biol Commun. 2015; 
Crespi GA, Ascher DB, Parker MW, Miles LA.
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Molecular Biology Reagents … The first construct to yield diffracting crystals was Fab expressed with a C-terminal hexa-His-tagged heavy chain. 2.1. Expression and purification. We obtained synthetic DNA cloned into pcDNA3.1 expression vectors from GenScript for expression of the heavy and light chains … Get A Quote

摘要

Bapineuzumab (AAB-001) and its derivative (AAB-003) are humanized versions of the anti-Aβ murine antibody 3D6 and are immunotherapy candidates in Alzheimer's disease. The common Fab fragment of these immunotherapies has been expressed, purified and crystallized in complex with β-amyloid peptides (residues 1-8 and 1-28). Diffraction data at high resolution were acquired from crystals of Fab-Aβ8 (2.0 Å) and Fab-Aβ28 (2.2 Å) complexes at the Australian Synchrotron. Both crystal forms belonged to the primitive orthorhombic space group P21221.

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