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

Journal Article · · Acta Crystallographica. Section F
;  [1];  [1]
  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, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 4 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English