Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Expression, purification and crystallization of two major envelope proteins from white spot syndrome virus

Expression, purification and crystallization of two major envelope proteins from white spot... White spot syndrome virus (WSSV) is a major virulent pathogen known to infect penaeid shrimp and other crustaceans. VP26 and VP28, two major envelope proteins from WSSV, have been identified and overexpressed in Escherichia coli. In order to facilitate purification and crystallization, predicted N‐terminal transmembrane regions of approximately 35 amino acids have been truncated from both VP26 and VP28. Truncated VP26 and VP28 and their corresponding SeMet‐labelled proteins were purified and the SeMet proteins were crystallized by the hanging‐drop vapour‐diffusion method. Crystals of SeMet‐labelled VP26 were obtained using a reservoir consisting of 0.1 M citric acid pH 3.5, 3.0 M sodium chloride and 1%(w/v) polyethylene glycol 3350, whereas SeMet VP28 was crystallized using a reservoir solution consisting of 25% polyethylene glycol 8000, 0.2 M calcium acetate, 0.1 M Na HEPES pH 7.5 and 1.5%(w/v) 1,2,3‐heptanetriol. Crystals of SeMet‐labelled VP26 diffract to 2.2 Å resolution and belong to space group R32, with unit‐cell parameters a = b = 73.92, c = 199.31 Å. SeMet‐labelled VP28 crystallizes in space group P212121, with unit‐cell parameters a = 105.33, b = 106.71, c = 200.37 Å, and diffracts to 2.0 Å resolution. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Expression, purification and crystallization of two major envelope proteins from white spot syndrome virus

Loading next page...
 
/lp/wiley/expression-purification-and-crystallization-of-two-major-envelope-cMoLA00XrG

References (10)

Publisher
Wiley
Copyright
Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309107029351
pmid
17620728
Publisher site
See Article on Publisher Site

Abstract

White spot syndrome virus (WSSV) is a major virulent pathogen known to infect penaeid shrimp and other crustaceans. VP26 and VP28, two major envelope proteins from WSSV, have been identified and overexpressed in Escherichia coli. In order to facilitate purification and crystallization, predicted N‐terminal transmembrane regions of approximately 35 amino acids have been truncated from both VP26 and VP28. Truncated VP26 and VP28 and their corresponding SeMet‐labelled proteins were purified and the SeMet proteins were crystallized by the hanging‐drop vapour‐diffusion method. Crystals of SeMet‐labelled VP26 were obtained using a reservoir consisting of 0.1 M citric acid pH 3.5, 3.0 M sodium chloride and 1%(w/v) polyethylene glycol 3350, whereas SeMet VP28 was crystallized using a reservoir solution consisting of 25% polyethylene glycol 8000, 0.2 M calcium acetate, 0.1 M Na HEPES pH 7.5 and 1.5%(w/v) 1,2,3‐heptanetriol. Crystals of SeMet‐labelled VP26 diffract to 2.2 Å resolution and belong to space group R32, with unit‐cell parameters a = b = 73.92, c = 199.31 Å. SeMet‐labelled VP28 crystallizes in space group P212121, with unit‐cell parameters a = 105.33, b = 106.71, c = 200.37 Å, and diffracts to 2.0 Å resolution.

Journal

Acta Crystallographica Section FWiley

Published: Jul 1, 2007

There are no references for this article.