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Crystallization of hepatitis B virus core protein shells: determination of cryoprotectant conditions and preliminary X‐ray characterization

Crystallization of hepatitis B virus core protein shells: determination of cryoprotectant... Hepatitis B virus causes liver cirrhosis and hepatocellular cancer and is a major cause of death, particularly in Asia and sub‐Saharan Africa. The virus consists of an inner core or nucleocapsid, which encloses the viral nucleic acid, with an outer lipid envelope containing surface‐antigen proteins. The core protein, when expressed in E. coli, assembles into spherical shells containing 180 or 240 subunits, arranged with T = 3 or T = 4 icosahedral symmetry. The C‐terminal region of the protein is involved in nucleic acid binding, and deletion of this region does not prevent capsid formation. C‐terminally deleted hepatitis B core shells containing 240 subunits have been crystallized and data has been collected to 3.6 Å resolution from frozen crystals, using butanediol as a cryoprotectant. The crystals have C2 symmetry, with unit‐cell parameters a = 538.0, b = 353.0, c = 369.6 Å, β = 132.3°. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section D Wiley

Crystallization of hepatitis B virus core protein shells: determination of cryoprotectant conditions and preliminary X‐ray characterization

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Publisher
Wiley
Copyright
Copyright © 1999 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1399-0047
eISSN
1399-0047
DOI
10.1107/S0907444998012621
Publisher site
See Article on Publisher Site

Abstract

Hepatitis B virus causes liver cirrhosis and hepatocellular cancer and is a major cause of death, particularly in Asia and sub‐Saharan Africa. The virus consists of an inner core or nucleocapsid, which encloses the viral nucleic acid, with an outer lipid envelope containing surface‐antigen proteins. The core protein, when expressed in E. coli, assembles into spherical shells containing 180 or 240 subunits, arranged with T = 3 or T = 4 icosahedral symmetry. The C‐terminal region of the protein is involved in nucleic acid binding, and deletion of this region does not prevent capsid formation. C‐terminally deleted hepatitis B core shells containing 240 subunits have been crystallized and data has been collected to 3.6 Å resolution from frozen crystals, using butanediol as a cryoprotectant. The crystals have C2 symmetry, with unit‐cell parameters a = 538.0, b = 353.0, c = 369.6 Å, β = 132.3°.

Journal

Acta Crystallographica Section DWiley

Published: Feb 1, 1999

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