Crystallization and preliminary crystallographic analysis of the fusion core of the spike protein of the murine coronavirus mouse hepatitis virus (MHV).
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%.
Xu
Yanhui
Y
Laboratory of Structural Biology, Tsinghua University, Beijing 100084, People's Republic of China.
Bai
Zhihong
Z
Qin
Lan
L
Li
Xu
X
Gao
George
G
Rao
Zihe
Z
D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D006517:Murine hepatitis virus / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins / Q000737:chemistry*
D008562:Membrane Glycoproteins; D011994:Recombinant Proteins; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins