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EC Number	Crystallization (Commentary)
3.6.1.B17	comparison of crystal structures of the full-length NS3 from Dengue virus and Hepatitis C virus indicates a major difference in the relative orientations between the protease and helicase domains in the two proteins. Specifically, a beta-strand in the HCV NS3 clamps the protease domain next to the helicase domain, thereby creating a compact conformational state that differs from the extended conformation observed in the DENV protein
3.6.1.B17	enzyme in complex with ADP, using 200 mM NaCl, 20% (w/v) PEG 4000, 100 mM Tris pH 8.0

EC Number

Crystallization (Commentary)

3.6.1.B17

comparison of crystal structures of the full-length NS3 from Dengue virus and Hepatitis C virus indicates a major difference in the relative orientations between the protease and helicase domains in the two proteins. Specifically, a beta-strand in the HCV NS3 clamps the protease domain next to the helicase domain, thereby creating a compact conformational state that differs from the extended conformation observed in the DENV protein

3.6.1.B17

enzyme in complex with ADP, using 200 mM NaCl, 20% (w/v) PEG 4000, 100 mM Tris pH 8.0

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Release 2023.1 (January 2023)