Open AccessCrystallization and preliminary crystallographic analysis of the heptad‐repeat complex of SARS coronavirus spike protein
Author(s) -
Xu Yanhui,
Su Nan,
Qin Lan,
Bai Zhihong,
Gao George F.,
Rao Zihe
Publication year - 2004
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904027258
Subject(s) - heptad repeat , coronaviridae , crystallography , coronavirus , crystallization , virology , biology , lipid bilayer fusion , virus , chemistry , biophysics , peptide sequence , covid-19 , medicine , genetics , gene , disease , organic chemistry , pathology , infectious disease (medical specialty)
The aetiological agent of an emergent outbreak of atypical pneumonia, severe acute respiratory syndrome (SARS), is a positive‐stranded RNA virus (SARS‐CoV) belonging to the Coronaviridae family with a genome that differs substantially from those of other known coronaviruses. Highly conserved heptad‐repeat (HR1 and HR2) regions in class I viral fusion proteins, including spike protein from SARS coronavirus, interact with each other to form a six‐helix bundle, which is called a fusion core. The crystal structure of the fusion core is expected to greatly facilitate drug design. Crystals of the fusion core of SARS‐CoV spike protein 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. The crystals have unit‐cell parameters a = 121.2, b = 66.3, c = 70.0 Å, α = γ = 90, β = 107.4° and belong to space group C 2. Assuming the presence of six molecules per asymmetric unit, the solvent content is estimated to be about 28%.