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

doi:10.1107/S0907444997008883

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

Department of Chemistry & Nanoscience

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

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 language	English
Pages (from-to)	121-123
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	54
Issue number	1
DOIs	https://doi.org/10.1107/S0907444997008883
State	Published - 1 Jan 1998

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

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 {\AA}. The asymmetric unit contains one molecule of the helicase domain, with the crystal volume per protein mass (V(m)) of 2.50 {\AA}3 Da-1 and solvent content of about 50.8% by volume. A native data set to 2.3 {\AA} resolution was obtained from a frozen crystal indicating that the crystals are quite suitable for structure determination by multiple isomorphous replacement.",

author = "Kang, {Lin Woo} and Cho, {Hyun Soo} and Cha, {Sun Shin} and Chung, {Kyung Min} and Back, {Sung Hoon} and Jang, {Sung Key} and Oh, {Byung Ha}",

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AU - Kang, Lin Woo

AU - Cho, Hyun Soo

AU - Cha, Sun Shin

AU - Chung, Kyung Min

AU - Back, Sung Hoon

AU - Jang, Sung Key

AU - Oh, Byung Ha

PY - 1998/1/1

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N2 - 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.

AB - 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.

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

Abstract

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