id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-285039-9piio754	Zhou, Haixia	Crystallization and Structural Determination of the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein	2019-09-14		.txt	text/plain	1940	144	61	Three-dimensional structures of the receptor-binding domain (RBD) of MERS-CoV spike glycoprotein bound to cellular receptor and monoclonal antibodies (mAbs) have been determined by X-ray crystallography, providing structural information about receptor recognition and neutralizing mechanisms of mAbs at the atomic level. The first three-dimensional structure of the MERS-CoV spike glycoprotein receptor-binding domain (RBD), providing the molecular basis of viral attachment to host cells, was determined in the complex with it cellular receptor dipeptidyl peptidase 4 (DPP4, also called CD26) by X-ray crystallography [1] . After obtaining the phases of these diffracted X-rays by heavy-atom derivative, anomalous scattering or molecular replacement methods, a protein crystallographer then calculates the density of electrons with the protein crystal and builds a structural model based on the density map. MER-CoV RBD can be expressed using the Bac-to-Bac baculovirus expression system (Fig. 1 ), collected and captured using NTA Sepharose (GE Healthcare) and then further purified by gel filtration chromatography using a Superdex 200 High Performance column (GE Healthcare).	./cache/cord-285039-9piio754.txt	./txt/cord-285039-9piio754.txt