title: The flavivirus envelope protein E: isolation of a soluble form from tick-borne encephalitis virus and its crystallization.
abstract: By the use of limited trypsin digestion of purified virions, we generated a membrane anchor-free and crystallizable form of the tick-borne encephalitis virus envelope glycoprotein E. It retained its reactivity with a panel of monoclonal antibodies, and only subtle structural differences from the native protein E were recognized. Treatment with the bifunctional cross-linker dimethylsuberimidate resulted in the formation of a dimer. Crystallization experiments yielded hexagonal rod-shaped crystals suitable for X-ray diffraction analysis.
authors.affiliation: Institute of Virology, University of Vienna, Austria.
authors.forename: F X
authors.initials: FX
authors.lastname: Heinz
authors.forename: C W
authors.initials: CW
authors.lastname: Mandl
authors.forename: H
authors.initials: H
authors.lastname: Holzmann
authors.forename: C
authors.initials: C
authors.lastname: Kunz
authors.forename: B A
authors.initials: BA
authors.lastname: Harris
authors.forename: F
authors.initials: F
authors.lastname: Rey
authors.forename: S C
authors.initials: SC
authors.lastname: Harrison
mesh_terms: D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D004669:Encephalitis Viruses, Tick-Borne / Q000737:chemistry*; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000032:analysis; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D014357:Trypsin; D014759:Viral Envelope Proteins / Q000276:immunology / Q000302:isolation & purification*; D014771:Virion / Q000737:chemistry*
chemical_list: D000939:Epitopes; D010446:Peptide Fragments; D014759:Viral Envelope Proteins; C065696:glycoprotein E, Flavivirus; D014357:Trypsin