Open AccessCrystallization and preliminary crystallographic analysis of the fusion core of the spike protein of the murine coronavirus mouse hepatitis virus (MHV)
Author(s) -
Xu Yanhui,
Bai Zhihong,
Qin Lan,
Li Xu,
Gao George,
Rao Zihe
Publication year - 2004
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904020517
Subject(s) - crystallography , crystallization , derivative (finance) , crystal (programming language) , crystal structure , resolution (logic) , molecule , capsid , x ray crystallography , diffraction , chemistry , materials science , virus , physics , virology , optics , biology , organic chemistry , artificial intelligence , computer science , financial economics , economics , programming language
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 Å 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 Å 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 Å, α = β = 90, γ = 120° and belong to space group R 3. Assuming the presence of two molecules in the asymmetric unit, the solvent content is calculated to be about 46%.