Crystallization and preliminary X-ray crystallographic analysis of the helicase domain of hepatitis C virus NS3 protein

Lin Woo Kang, Hyun Soo Cho, Sun Shin Cha, Kyung Min Chung, Sung Hoon Back, Sung Key Jang, Byung Ha Oh

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The NS3 protein of hepatitis C virus (HCV) is thought to be essential for vital replication. The N-terminal domain of the protein contains protease activity and the C-terminal domain contains nucleotide triphosphatase and RNA helicase activity. The RNA helicase domain of HCV NS3 protein was purified by using affinity-column chromatographic methods, and crystallized by using the microbatch crystallization method under oil at 277 K. The crystals belong to primitive trigonal space group P3121 or P3221 with cell dimensions of a = b = 93.3, c = 104.6 Å. The asymmetric unit contains one molecule of the helicase domain, with the crystal volume per protein mass (V(m)) of 2.50 Å3 Da-1 and solvent content of about 50.8% by volume. A native data set to 2.3 Å resolution was obtained from a frozen crystal indicating that the crystals are quite suitable for structure determination by multiple isomorphous replacement.

Original languageEnglish
Pages (from-to)121-123
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume54
Issue number1
DOIs
Publication statusPublished - 1998 Jan 1

All Science Journal Classification (ASJC) codes

  • Structural Biology

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