NDLI: Expression, crystallization and preliminary crystallographic study of mouse hepatitis virus (MHV) nucleocapsid protein C-terminal domain.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tong, Xiaohang Ma, Yanlin Li, Xuemei
Description	Author Affiliation: Tong X ( National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, People's Republic of China.)
Abstract	Mouse hepatitis virus (MHV) belongs to the group II coronaviruses. The virus produces nine genes encoding 11 proteins that could be recognized as structural proteins and nonstructural proteins and are crucial for viral RNA synthesis. The nucleocapsid (N) protein, one of the structural proteins, interacts with the 30.4 kb virus genomic RNA to form the helical nucleocapsid and associates with the membrane glycoprotein via its C-terminus to stabilize virion assembly. Here, the expression and crystallization of the MHV nucleocapsid protein C-terminal domain are reported. The crystals diffracted to 2.20 A resolution and belonged to space group P422, with unit-cell parameters a = 66.6, c = 50.8 A. Assuming the presence of two molecules in the asymmetric unit, the solvent content is 43.0% (V(M) = 2.16 A(3) Da(-1)).
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
DOI	10.1107/S1744309110012492
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 6
Volume Number	66
Language	English
Publisher	Wiley
Publisher Date	2010-06-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Murine Hepatitis Virus Chemistry Nucleocapsid Proteins Crystallization Crystallography, X-ray Gene Expression Genetics Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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