Expression, crystallization and preliminary crystallographic data analysis of filamin a repeats 14-16

Adeleke Halilu Aguda; Amos Malle Sakwe; Lars Rask; Robert Charles Robinson

doi:10.1107/S1744309107006689

Expression, crystallization and preliminary crystallographic data analysis of filamin a repeats 14-16

Adeleke Halilu Aguda, Amos Malle Sakwe, Lars Rask, Robert Charles Robinson

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

1 Citation (Scopus)

Abstract

Human filamin A is a 280 kDa protein involved in actin-filament cross-linking. It is structurally divided into an actin-binding headpiece (ABD) and a rod domain containing 24 immunoglobulin-like (Ig) repeats. A fragment of human filamin A (Ig repeats 14-16) was cloned and expressed in Escherichia coli and the purified protein was crystallized in 1.6 M ammonium sulfate, 2% PEG 1000 and 100 mM HEPES pH 7.5. The crystals diffracted to 1.95 Å and belong to space group P2₁2₁2₁, with unit-cell parameters a = 50.63, b = 52.10, c = 98.46 Å, α = β = γ = 90°.

Original language	English
Pages (from-to)	291-293
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	63
Issue number	4
DOIs	https://doi.org/10.1107/S1744309107006689
Publication status	Published - 2007
Externally published	Yes

Keywords

ABP-280
Calponin homology
Cytoskeleton
Filamin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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title = "Expression, crystallization and preliminary crystallographic data analysis of filamin a repeats 14-16",

abstract = "Human filamin A is a 280 kDa protein involved in actin-filament cross-linking. It is structurally divided into an actin-binding headpiece (ABD) and a rod domain containing 24 immunoglobulin-like (Ig) repeats. A fragment of human filamin A (Ig repeats 14-16) was cloned and expressed in Escherichia coli and the purified protein was crystallized in 1.6 M ammonium sulfate, 2% PEG 1000 and 100 mM HEPES pH 7.5. The crystals diffracted to 1.95 {\AA} and belong to space group P212121, with unit-cell parameters a = 50.63, b = 52.10, c = 98.46 {\AA}, α = β = γ = 90°.",

keywords = "ABP-280, Calponin homology, Cytoskeleton, Filamin",

author = "Aguda, {Adeleke Halilu} and Sakwe, {Amos Malle} and Lars Rask and Robinson, {Robert Charles}",

year = "2007",

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language = "English",

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pages = "291--293",

journal = "Acta Crystallographica Section F:Structural Biology Communications",

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T1 - Expression, crystallization and preliminary crystallographic data analysis of filamin a repeats 14-16

AU - Aguda, Adeleke Halilu

AU - Sakwe, Amos Malle

AU - Rask, Lars

AU - Robinson, Robert Charles

PY - 2007

Y1 - 2007

N2 - Human filamin A is a 280 kDa protein involved in actin-filament cross-linking. It is structurally divided into an actin-binding headpiece (ABD) and a rod domain containing 24 immunoglobulin-like (Ig) repeats. A fragment of human filamin A (Ig repeats 14-16) was cloned and expressed in Escherichia coli and the purified protein was crystallized in 1.6 M ammonium sulfate, 2% PEG 1000 and 100 mM HEPES pH 7.5. The crystals diffracted to 1.95 Å and belong to space group P212121, with unit-cell parameters a = 50.63, b = 52.10, c = 98.46 Å, α = β = γ = 90°.

AB - Human filamin A is a 280 kDa protein involved in actin-filament cross-linking. It is structurally divided into an actin-binding headpiece (ABD) and a rod domain containing 24 immunoglobulin-like (Ig) repeats. A fragment of human filamin A (Ig repeats 14-16) was cloned and expressed in Escherichia coli and the purified protein was crystallized in 1.6 M ammonium sulfate, 2% PEG 1000 and 100 mM HEPES pH 7.5. The crystals diffracted to 1.95 Å and belong to space group P212121, with unit-cell parameters a = 50.63, b = 52.10, c = 98.46 Å, α = β = γ = 90°.

KW - ABP-280

KW - Calponin homology

KW - Cytoskeleton

KW - Filamin

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JF - Acta Crystallographica Section F:Structural Biology Communications

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Expression, crystallization and preliminary crystallographic data analysis of filamin a repeats 14-16

Abstract

Keywords

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