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Crystallization and preliminary crystallographic studies of the cofactor-binding domain of the LysR-type transcriptional regulator Cbl from Escherichia coli

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Crystallization and preliminary crystallographic studies of the cofactor-binding domain of the LysR-type transcriptional regulator Cbl from Escherichia coli. / Stec, E ; Witkowska, M ; Hryniewicz, M M ; Brzozowski, A M ; Wilkinson, A J ; Bujacz, G D .

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 60, 09.2004, p. 1654-1657.

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Harvard

Stec, E, Witkowska, M, Hryniewicz, MM, Brzozowski, AM, Wilkinson, AJ & Bujacz, GD 2004, 'Crystallization and preliminary crystallographic studies of the cofactor-binding domain of the LysR-type transcriptional regulator Cbl from Escherichia coli', Acta Crystallographica Section D: Biological Crystallography, vol. 60, pp. 1654-1657. https://doi.org/10.1107/S0907444904016841

APA

Stec, E., Witkowska, M., Hryniewicz, M. M., Brzozowski, A. M., Wilkinson, A. J., & Bujacz, G. D. (2004). Crystallization and preliminary crystallographic studies of the cofactor-binding domain of the LysR-type transcriptional regulator Cbl from Escherichia coli. Acta Crystallographica Section D: Biological Crystallography, 60, 1654-1657. https://doi.org/10.1107/S0907444904016841

Vancouver

Stec E, Witkowska M, Hryniewicz MM, Brzozowski AM, Wilkinson AJ, Bujacz GD. Crystallization and preliminary crystallographic studies of the cofactor-binding domain of the LysR-type transcriptional regulator Cbl from Escherichia coli. Acta Crystallographica Section D: Biological Crystallography. 2004 Sep;60:1654-1657. https://doi.org/10.1107/S0907444904016841

Author

Stec, E ; Witkowska, M ; Hryniewicz, M M ; Brzozowski, A M ; Wilkinson, A J ; Bujacz, G D . / Crystallization and preliminary crystallographic studies of the cofactor-binding domain of the LysR-type transcriptional regulator Cbl from Escherichia coli. In: Acta Crystallographica Section D: Biological Crystallography. 2004 ; Vol. 60. pp. 1654-1657.

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@article{543f455a85954dbeabefaef9b55c8aa2,
title = "Crystallization and preliminary crystallographic studies of the cofactor-binding domain of the LysR-type transcriptional regulator Cbl from Escherichia coli",
abstract = "Cbl (CysB-like protein) is a member of the family of LysR-type transcriptional regulators (LTTRs) and controls genes engaged in sulfur assimilation in Escherichia coli. It has been postulated that adenosine 5-phosphosulfate (APS) is responsible for abolishing Cbl-activated transcription from the ssu promoter (Bykowski et al., 2002). To elucidate the structural basis of Cbl function and to confirm the role of APS as an anti-inducer, the cofactor-binding domain of Cbl (c-Cbl, MW = 26 kDa) was cloned, purified and crystallized in the presence of APS. The crystals belong to space group C222(1), but show substantial variation of the unit-cell parameters and diffraction anisotropy. Despite this, X-ray data extending to 3.0 Angstrom resolution have been collected and solution of the structure by molecular replacement is in progress.",
keywords = "FAMILY, PROTEINS, SULFUR, SWITCH, MEMBER, CYSB, GENE",
author = "E Stec and M Witkowska and Hryniewicz, {M M} and Brzozowski, {A M} and Wilkinson, {A J} and Bujacz, {G D}",
year = "2004",
month = "9",
doi = "10.1107/S0907444904016841",
language = "English",
volume = "60",
pages = "1654--1657",
journal = "Acta Crystallographica Section D: Biological Crystallography",
issn = "0907-4449",
publisher = "International Union of Crystallography",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Crystallization and preliminary crystallographic studies of the cofactor-binding domain of the LysR-type transcriptional regulator Cbl from Escherichia coli

AU - Stec, E

AU - Witkowska, M

AU - Hryniewicz, M M

AU - Brzozowski, A M

AU - Wilkinson, A J

AU - Bujacz, G D

PY - 2004/9

Y1 - 2004/9

N2 - Cbl (CysB-like protein) is a member of the family of LysR-type transcriptional regulators (LTTRs) and controls genes engaged in sulfur assimilation in Escherichia coli. It has been postulated that adenosine 5-phosphosulfate (APS) is responsible for abolishing Cbl-activated transcription from the ssu promoter (Bykowski et al., 2002). To elucidate the structural basis of Cbl function and to confirm the role of APS as an anti-inducer, the cofactor-binding domain of Cbl (c-Cbl, MW = 26 kDa) was cloned, purified and crystallized in the presence of APS. The crystals belong to space group C222(1), but show substantial variation of the unit-cell parameters and diffraction anisotropy. Despite this, X-ray data extending to 3.0 Angstrom resolution have been collected and solution of the structure by molecular replacement is in progress.

AB - Cbl (CysB-like protein) is a member of the family of LysR-type transcriptional regulators (LTTRs) and controls genes engaged in sulfur assimilation in Escherichia coli. It has been postulated that adenosine 5-phosphosulfate (APS) is responsible for abolishing Cbl-activated transcription from the ssu promoter (Bykowski et al., 2002). To elucidate the structural basis of Cbl function and to confirm the role of APS as an anti-inducer, the cofactor-binding domain of Cbl (c-Cbl, MW = 26 kDa) was cloned, purified and crystallized in the presence of APS. The crystals belong to space group C222(1), but show substantial variation of the unit-cell parameters and diffraction anisotropy. Despite this, X-ray data extending to 3.0 Angstrom resolution have been collected and solution of the structure by molecular replacement is in progress.

KW - FAMILY

KW - PROTEINS

KW - SULFUR

KW - SWITCH

KW - MEMBER

KW - CYSB

KW - GENE

U2 - 10.1107/S0907444904016841

DO - 10.1107/S0907444904016841

M3 - Article

VL - 60

SP - 1654

EP - 1657

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

SN - 0907-4449

ER -