Preliminary crystallographic study of bluetongue virus capsid protein, VP7

A K Basak; D I Stuart; P Roy

doi:10.1016/0022-2836(92)90850-j

Preliminary crystallographic study of bluetongue virus capsid protein, VP7

J Mol Biol. 1992 Nov 20;228(2):687-9. doi: 10.1016/0022-2836(92)90850-j.

Authors

A K Basak¹, D I Stuart, P Roy

Affiliation

¹ Laboratory of Molecular Biophysics, Oxford, U.K.

PMID: 1333534
DOI: 10.1016/0022-2836(92)90850-j

Abstract

Bluetongue virus serotype 10 (BTV-10) VP7, expressed by insect cells infected with the recombinant baculovirus, has been purified and crystallized. Two crystal forms suitable for X-ray analysis have been obtained. Type I crystals belong to space group P6(3)22 with a = b = 95.2 A, c = 181.0 A, alpha = beta = 90 degrees gamma = 120.0 degrees, and contain a single subunit in the crystallographic asymmetric unit. They diffract to dmin = 3.0 A. Type II crystals belong to space group P2(1) with a = 69.4 A, b = 97.1 A, c = 71.4 A, beta = 109.0 degrees, and contain a trimer in the crystallographic asymmetric unit. They diffract to dmin = 2.1 A. These results, together with solution studies, show that the molecule is a trimer.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bluetongue virus / chemistry*
Viral Core Proteins / chemistry*
X-Ray Diffraction

Substances

Viral Core Proteins
VP7 protein, orbivirus