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Expression, purification and crystallization of the ectodomain of the envelope glycoprotein E2 from Bovine viral diarrhoea virus

Iourin, O., Harlos, K., El Omari, K., Lu, W., Kadlec, J., Iqbal, M., Meier, C., Palmer, A., Jones, I., Thomas, C., Brownlie, J., Grimes, J. M. and Stuart, D. I. (2013) Expression, purification and crystallization of the ectodomain of the envelope glycoprotein E2 from Bovine viral diarrhoea virus. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69 (1). pp. 35-38. ISSN 1744-3091

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To link to this item DOI: 10.1107/S1744309112049184

Abstract/Summary

Bovine viral diarrhoea virus (BVDV) is an economically important animal pathogen which is closely related to Hepatitis C virus. Of the structural proteins, the envelope glycoprotein E2 of BVDV is the major antigen which induces neutralizing antibodies; thus, BVDV E2 is considered as an ideal target for use in subunit vaccines. Here, the expression, purification of wild-type and mutant forms of the ectodomain of BVDV E2 and subsequent crystallization and data collection of two crystal forms grown at low and neutral pH are reported. Native and multiple-wavelength anomalous dispersion (MAD) data sets have been collected and structure determination is in progress.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences > Biomedical Sciences
ID Code:31534
Publisher:International Union of Crystallography

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