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

Journal Article · Sun Apr 01 00:00:00 EDT 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309107006689· OSTI ID:22360291

Sakwe, Amos Malle; Rask, Lars ^[1]; Robinson, Robert Charles ^[1]

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1. Department of Medical Biochemistry and Microbiology, Uppsala University (Sweden)

The crystallization and crystallographic data analysis of filamin repeats 14–16 are reported. 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 P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 50.63, b = 52.10, c = 98.46 Å, α = β = γ = 90°.

• OSTI ID: 22360291
• Journal Information: Acta Crystallographica. Section F, Vol. 63, Issue Pt 4; Other Information: PMCID: PMC2330200; PMID: 17401197; PUBLISHER-ID: bo5013; OAI: oai:pubmedcentral.nih.gov:2330200; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

36 MATERIALS SCIENCE
75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
60 APPLIED LIFE SCIENCES
AMMONIUM SULFATES
CROSS-LINKING
CRYSTALLIZATION
CRYSTALS
DATA ANALYSIS
ESCHERICHIA COLI
FILAMENTS
MICROTUBULES
RODS
SPACE GROUPS