Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS)

Marco Nardini; Stefania Spanò; Claudia Cericola; Alessandra Pesce; Gianluca Damonte; Alberto Luini; Daniela Corda; Martino Bolognesi

doi:10.1107/S0907444902006984

Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS)

Marco Nardini, Stefania Spanò, Claudia Cericola, Alessandra Pesce, Gianluca Damonte, Alberto Luini, Daniela Corda, Martino Bolognesi

IRCCS SDN

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

Abstract

Brefeldin A-ADP ribosylated substrate (BARS) is a newly discovered enzyme involved in membrane fission, catalyzing the formation of phosphatidic acid by transfer of an acyl group from acyl-CoA to lysophosphatidic acid. A truncated form of BARS, lacking the C-terminal segment expected to interact with the Golgi membrane, has been expressed in soluble form in Escherichia coli, purified and crystallized. BARS crystals diffract up to 2.5 Å resolution using synchrotron radiation and belong to space group P6₂22/P6₄22, with unit-cell parameters a = b = 89.2, c = 162.6 Å, α = β = 90, γ = 120° and one molecule (39.5 kDa) per asymmetric unit. SeMet-substituted BARS has been crystallized under growth conditions very similar to those of the native protein.

Original language	English
Pages (from-to)	1068-1070
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	58
Issue number	6 II
DOIs	https://doi.org/10.1107/S0907444902006984
Publication status	Published - 2002

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Biochemistry
Biophysics
Clinical Biochemistry
Structural Biology
Condensed Matter Physics

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Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS). / Nardini, Marco; Spanò, Stefania; Cericola, Claudia; Pesce, Alessandra; Damonte, Gianluca; Luini, Alberto; Corda, Daniela; Bolognesi, Martino.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 58, No. 6 II, 2002, p. 1068-1070.

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

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title = "Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS)",

abstract = "Brefeldin A-ADP ribosylated substrate (BARS) is a newly discovered enzyme involved in membrane fission, catalyzing the formation of phosphatidic acid by transfer of an acyl group from acyl-CoA to lysophosphatidic acid. A truncated form of BARS, lacking the C-terminal segment expected to interact with the Golgi membrane, has been expressed in soluble form in Escherichia coli, purified and crystallized. BARS crystals diffract up to 2.5 {\AA} resolution using synchrotron radiation and belong to space group P6222/P6422, with unit-cell parameters a = b = 89.2, c = 162.6 {\AA}, α = β = 90, γ = 120° and one molecule (39.5 kDa) per asymmetric unit. SeMet-substituted BARS has been crystallized under growth conditions very similar to those of the native protein.",

author = "Marco Nardini and Stefania Span{\`o} and Claudia Cericola and Alessandra Pesce and Gianluca Damonte and Alberto Luini and Daniela Corda and Martino Bolognesi",

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T1 - Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS)

AU - Nardini, Marco

AU - Spanò, Stefania

AU - Cericola, Claudia

AU - Pesce, Alessandra

AU - Damonte, Gianluca

AU - Luini, Alberto

AU - Corda, Daniela

AU - Bolognesi, Martino

PY - 2002

Y1 - 2002

N2 - Brefeldin A-ADP ribosylated substrate (BARS) is a newly discovered enzyme involved in membrane fission, catalyzing the formation of phosphatidic acid by transfer of an acyl group from acyl-CoA to lysophosphatidic acid. A truncated form of BARS, lacking the C-terminal segment expected to interact with the Golgi membrane, has been expressed in soluble form in Escherichia coli, purified and crystallized. BARS crystals diffract up to 2.5 Å resolution using synchrotron radiation and belong to space group P6222/P6422, with unit-cell parameters a = b = 89.2, c = 162.6 Å, α = β = 90, γ = 120° and one molecule (39.5 kDa) per asymmetric unit. SeMet-substituted BARS has been crystallized under growth conditions very similar to those of the native protein.

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