Faculty Collaboration Database

Crystallization and preliminary X-ray crystallographic analysis of the trimer core from measles virus fusion protein. Acta Crystallogr D Biol Crystallogr 2003 Mar;59(Pt 3):587-90

Date

02/22/2003

Pubmed ID

12595734

DOI

10.1107/s0907444903001057

Scopus ID

2-s2.0-0037350119 (requires institutional sign-in at Scopus site)   11 Citations

Abstract

Two heptad-repeat regions (HR1 and HR2) are highly conserved in paramyxovirus fusion proteins and form a stable helical trimer of heterodimers [(HR1-HR2)(3)] after the fusion between viral and cellular membranes. In this study, two HR regions of the fusion protein of measles virus, a member of the paramyxoviruses, were selected and overexpressed as a single chain (named 2-Helix) connected by an amino-acid linker using a GST-fusion expression system in Escherichia coli. Crystals of 2-Helix protein (GST removed) could be obtained from many conditions using the sitting- or hanging-drop vapour-diffusion method. A complete data set was collected in-house to 1.9 A resolution from a single crystal. The crystal belongs to space group P6, with unit-cell parameters a = b = 51.637, c = 67.058 A. To facilitate the crystal structure solution, SeMet-substituted 2-Helix crystals, grown under similar conditions to the native, were also obtained and diffracted X-rays to 1.8 A using synchrotron radiation.

Author List

Zhu J, Ding Y, Gao F, Wu T, Zhang CW, Tien P, Rao Z, Gao GF

Author

Jieqing Zhu PhD Assistant Professor, Associate Investigator in the Biochemistry department at BloodCenter of Wisconsin

MESH terms used to index this publication - Major topics in bold

Crystallization
Crystallography, X-Ray
Escherichia coli
Gene Expression Regulation, Viral
Protein Conformation
Recombinant Proteins
Selenomethionine
Viral Fusion Proteins
X-Ray Diffraction