MersV1, PubMed, Corpus, bibRecord, 000314

Crystallization and Structural Determination of the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein.

Identifieur interne : 000314 ( PubMed/Corpus ); précédent : 000313; suivant : 000315

Crystallization and Structural Determination of the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein.

Auteurs : Haixia Zhou ; Shuyuan Zhang ; Xinquan Wang

Source :

Methods in molecular biology (Clifton, N.J.) [ 1940-6029 ] ; 2020.

RBID : pubmed:31883086

Abstract

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. In this chapter, we describe the purification, crystallization, and structure determination of the MERS-CoV RBD.

DOI: 10.1007/978-1-0716-0211-9_4
PubMed: 31883086

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<front><div type="abstract" xml:lang="en">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. In this chapter, we describe the purification, crystallization, and structure determination of the MERS-CoV RBD.</div>
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Crystallization and Structural Determination of the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein.

Crystallization and Structural Determination of the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein.

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