Preparation, crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC1692 from Xanthomonas campestris

Ko Hsin Chin; Zhao Wei Huang; Kun Chou Wei; Chia Cheng Chou; Cheng Chung Lee; Hui Lin Shr; Fei Philip Gao; Ping Chiang Lyu; Andrew H.J. Wang; Shan Ho Chou

doi:10.1107/S1744309105018798

Preparation, crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC1692 from Xanthomonas campestris

Ko Hsin Chin, Zhao Wei Huang, Kun Chou Wei, Chia Cheng Chou, Cheng Chung Lee, Hui Lin Shr, Fei Philip Gao, Ping Chiang Lyu, Andrew H.J. Wang, Shan Ho Chou

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

Abstract

Xanthomonas campestris pv. campestris strain 17 is a Gram-negative yellow-pigmented pathogenic bacterium that causes black rot, one of the major worldwide diseases of cruciferous crops. Its genome contains approximately 4500 genes, one third of which have no known structure and/or function yet are highly conserved among several different bacterial genuses. One of these gene products is XC1692 protein, containing 141 amino acids. It was overexpressed in Escherichia coli, purified and crystallized in a variety of forms using the hanging-drop vapour-diffusion method. The crystals diffract to at least 1.45 Å resolution. They are hexagonal and belong to space group P6₃, with unit-cell parameters a = b = 56.9, c = 71.0 Å. They contain one molecule per asymmetric unit.

Original language	English
Pages (from-to)	691-693
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	61
Issue number	7
DOIs	https://doi.org/10.1107/S1744309105018798
Publication status	Published - Jul 2005
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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10.1107/S1744309105018798

Cite this

Chin, K. H., Huang, Z. W., Wei, K. C., Chou, C. C., Lee, C. C., Shr, H. L., Gao, F. P., Lyu, P. C., Wang, A. H. J., & Chou, S. H. (2005). Preparation, crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC1692 from Xanthomonas campestris. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61(7), 691-693. https://doi.org/10.1107/S1744309105018798

Preparation, crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC1692 from Xanthomonas campestris. / Chin, Ko Hsin; Huang, Zhao Wei; Wei, Kun Chou et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 61, No. 7, 07.2005, p. 691-693.

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

Chin, KH, Huang, ZW, Wei, KC, Chou, CC, Lee, CC, Shr, HL, Gao, FP, Lyu, PC, Wang, AHJ & Chou, SH 2005, 'Preparation, crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC1692 from Xanthomonas campestris', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 61, no. 7, pp. 691-693. https://doi.org/10.1107/S1744309105018798

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title = "Preparation, crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC1692 from Xanthomonas campestris",

abstract = "Xanthomonas campestris pv. campestris strain 17 is a Gram-negative yellow-pigmented pathogenic bacterium that causes black rot, one of the major worldwide diseases of cruciferous crops. Its genome contains approximately 4500 genes, one third of which have no known structure and/or function yet are highly conserved among several different bacterial genuses. One of these gene products is XC1692 protein, containing 141 amino acids. It was overexpressed in Escherichia coli, purified and crystallized in a variety of forms using the hanging-drop vapour-diffusion method. The crystals diffract to at least 1.45 {\AA} resolution. They are hexagonal and belong to space group P63, with unit-cell parameters a = b = 56.9, c = 71.0 {\AA}. They contain one molecule per asymmetric unit.",

author = "Chin, {Ko Hsin} and Huang, {Zhao Wei} and Wei, {Kun Chou} and Chou, {Chia Cheng} and Lee, {Cheng Chung} and Shr, {Hui Lin} and Gao, {Fei Philip} and Lyu, {Ping Chiang} and Wang, {Andrew H.J.} and Chou, {Shan Ho}",

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AU - Chin, Ko Hsin

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AU - Lee, Cheng Chung

AU - Shr, Hui Lin

AU - Gao, Fei Philip

AU - Lyu, Ping Chiang

AU - Wang, Andrew H.J.

AU - Chou, Shan Ho

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AB - Xanthomonas campestris pv. campestris strain 17 is a Gram-negative yellow-pigmented pathogenic bacterium that causes black rot, one of the major worldwide diseases of cruciferous crops. Its genome contains approximately 4500 genes, one third of which have no known structure and/or function yet are highly conserved among several different bacterial genuses. One of these gene products is XC1692 protein, containing 141 amino acids. It was overexpressed in Escherichia coli, purified and crystallized in a variety of forms using the hanging-drop vapour-diffusion method. The crystals diffract to at least 1.45 Å resolution. They are hexagonal and belong to space group P63, with unit-cell parameters a = b = 56.9, c = 71.0 Å. They contain one molecule per asymmetric unit.

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Preparation, crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC1692 from Xanthomonas campestris

Abstract

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