Open AccessCrystallization and preliminary crystallographic analysis of the fusion core from two new zoonotic paramyxoviruses, Nipah virus and Hendra virus
Author(s) -
Xu Yanhui,
Lou Zhiyong,
Liu Yiwei,
Cole David K.,
Su Nan,
Qin Lan,
Li Xu,
Bai Zhihong,
Rao Zihe,
Gao George F.
Publication year - 2004
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904009515
Subject(s) - crystallography , crystallization , virus , derivative (finance) , hendra virus , lipid bilayer fusion , crystal (programming language) , chemistry , biology , virology , organic chemistry , financial economics , economics , ebola virus , computer science , programming language
Highly conserved heptad‐repeat (HR1 and HR2) regions in class I viral fusion (F) proteins, including the F protein from paramyxovirus, interact with each other post‐fusion to form a six‐helix bundle called a fusion core. Crystals of the fusion core of Nipah virus have been grown at 291 K using PEG 4000 as precipitant. The diffraction pattern of the crystal extends to 2.1 Å resolution at 100 K in‐house. The crystals have unit‐cell parameters a = 31.664, b = 31.725, c = 51.256 Å, α = 80.706, β = 86.343, γ = 65.812° and belong to space group P 1. Crystals of the fusion core of Hendra virus have also been grown at 291 K using PEG 4000 as precipitant. The diffraction pattern of the crystal extends to 2.0 Å resolution at 100 K in‐house. A selenomethionine (SeMet) derivative of the HeV fusion core was overexpressed using the same Escherichia coli expression system and purified. The derivative crystals were obtained under similar conditions and three different wavelength data sets were collected to 2.0 Å resolution from the derivative crystal at BSRF (Beijing Synchrotron Radiation Facility). The crystals have unit‐cell parameters a = 31.997, b = 31.970, c = 53.865 Å, α = 85.990, β = 85.842, γ = 68.245° and belong to space group P 1.