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. 1991 Oct;65(10):5579–5583. doi: 10.1128/jvi.65.10.5579-5583.1991

The flavivirus envelope protein E: isolation of a soluble form from tick-borne encephalitis virus and its crystallization.

F X Heinz 1, C W Mandl 1, H Holzmann 1, C Kunz 1, B A Harris 1, F Rey 1, S C Harrison 1
PMCID: PMC249068  PMID: 1716695

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.

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Selected References

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