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Homogeneously N-glycosylated proteins derived from the GlycoDelete HEK293 cell line enable diffraction-quality crystallogenesis

Acta Crystallogr D Struct Biol. 2020-11; 
Sandra Kozak, Yehudi Bloch, Steven De Munck, Aleksandra Mikula, Isabel Bento, Savvas N Savvides, Rob Meijers
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GenParts™ DNA Fragments … of human DSCAMIg7–Ig9, the DSCAM fragment covering resi- dues 595–884 was codon-optimized and synthesized by GenScript based on … at passage number 10 from a stock kindly provided by Nico Callewaert (VIB–UGent Center for Medical Biotechnology, Ghent, Belgium … Get A Quote

摘要

Structural studies of glycoproteins and their complexes provide critical insights into their roles in normal physiology and disease. Most glycoproteins contain N-linked glycosylation, a key post-translation modification that critically affects protein folding and stability and the binding kinetics underlying protein interactions. However, N-linked glycosylation is often an impediment to yielding homogeneous protein preparations for structure determination by X-ray crystallography or other methods. In particular, obtaining diffraction-quality crystals of such proteins and their complexes often requires modification of both the type of glycosylation patterns and their extent. Here, we demonstrate the benefits of ... More

关键词

GlycoDelete cell line, cell-surface receptors, crystallization, glycoproteins, glycosylation, synthetic biology