Crystallization and preliminary crystallographic analysis of the fusion core of the spike protein of the murine coronavirus mouse hepatitis virus (MHV).
Acta Crystallogr D Biol Crystallogr
; 60(Pt 11): 2013-5, 2004 Nov.
Article
em En
| MEDLINE
| ID: mdl-15502312
ABSTRACT
Crystals of a 2-Helix fusion-core construct of MHV spike protein (commonly referred to as E2) have been grown at 291 K using PEG 4000 as precipitant. The diffraction pattern of the crystal extends to 2.8 A resolution at 100 K in-house. Furthermore, a selenomethionine (SeMet) derivative of MHV spike protein fusion core has been overexpressed and purified. The derivative crystals were obtained under similar conditions and three different wavelength data sets were collected to 2.4 A resolution from a single derivative crystal at BSRF (Beijing Synchrotron Radiation Facility). The crystals have unit-cell parameters a = b = 48.3, c = 199.6 A, alpha = beta = 90, gamma = 120 degrees and belong to space group R3. Assuming the presence of two molecules in the asymmetric unit, the solvent content is calculated to be about 46%.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Glicoproteínas de Membrana
/
Proteínas do Envelope Viral
/
Vírus da Hepatite Murina
Idioma:
En
Ano de publicação:
2004
Tipo de documento:
Article