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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 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.63, b = 52.10, c = 98.46 A, alpha = beta = gamma = 90 degrees.

SUBMITTER: Aguda AH

PROVIDER: S-EPMC2330200 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature

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

Aguda Adeleke Halilu AH Sakwe Amos Malle AM Rask Lars L Robinson Robert Charles RC

Acta crystallographica. Section F, Structural biology and crystallization communications 20070312 Pt 4

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 A and belong to space group P2(1)2(1)2(1), with unit-cell p ...[more]

PMID: 17401197

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