| Literature DB >> 1716695 |
F X Heinz1, C W Mandl, H Holzmann, C Kunz, B A Harris, F Rey, S C Harrison.
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.Entities:
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Year: 1991 PMID: 1716695 PMCID: PMC249068
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103