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 journalArticle

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 languageEnglish
Pages (from-to)291-293
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number4
DOIs
Publication statusPublished - Dec 1 2007
Externally publishedYes

Fingerprint

Filamins
Crystallization
Immunoglobulins
Actins
crystallization
HEPES
proteins
ammonium sulfates
Escherichia coli Proteins
Ammonium Sulfate
Escherichia
Actin Cytoskeleton
Escherichia coli
filaments
Proteins
rods
fragments
Crystals
cells
crystals

Keywords

  • ABP-280
  • Calponin homology
  • Cytoskeleton
  • Filamin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics
  • Medicine(all)

Cite this

Expression, crystallization and preliminary crystallographic data analysis of filamin a repeats 14-16. / Aguda, Adeleke Halilu; Sakwe, Amos Malle; Rask, Lars; Robinson, Robert Charles.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 63, No. 4, 01.12.2007, p. 291-293.

Research output: Contribution to journalArticle

@article{292aa72001eb43bcaaef49fe6423a10a,
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",
month = "12",
day = "1",
doi = "10.1107/S1744309107006689",
language = "English",
volume = "63",
pages = "291--293",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
issn = "1744-3091",
publisher = "John Wiley and Sons Ltd",
number = "4",

}

TY - JOUR

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 - 2007/12/1

Y1 - 2007/12/1

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

UR - http://www.scopus.com/inward/record.url?scp=34249700179&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34249700179&partnerID=8YFLogxK

U2 - 10.1107/S1744309107006689

DO - 10.1107/S1744309107006689

M3 - Article

C2 - 17401197

AN - SCOPUS:34249700179

VL - 63

SP - 291

EP - 293

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

IS - 4

ER -