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

Abstract

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°.

Authors:
 [1];  [2]; ;  [1];  [1];  [2]
  1. Department of Medical Biochemistry and Microbiology, Uppsala University (Sweden)
  2. (Singapore)
Publication Date:
OSTI Identifier:
22360291
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal 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)
Country of Publication:
United Kingdom
Language:
English
Subject:
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

Citation Formats

Aguda, Adeleke Halilu, E-mail: adelekeha@imcb.a-star.edu.sg, Institute of Molecular and Cell Biology, Sakwe, Amos Malle, Rask, Lars, Robinson, Robert Charles, and Institute of Molecular and Cell Biology. Expression, crystallization and preliminary crystallographic data analysis of filamin A repeats 14–16. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107006689.
Aguda, Adeleke Halilu, E-mail: adelekeha@imcb.a-star.edu.sg, Institute of Molecular and Cell Biology, Sakwe, Amos Malle, Rask, Lars, Robinson, Robert Charles, & Institute of Molecular and Cell Biology. Expression, crystallization and preliminary crystallographic data analysis of filamin A repeats 14–16. United Kingdom. doi:10.1107/S1744309107006689.
Aguda, Adeleke Halilu, E-mail: adelekeha@imcb.a-star.edu.sg, Institute of Molecular and Cell Biology, Sakwe, Amos Malle, Rask, Lars, Robinson, Robert Charles, and Institute of Molecular and Cell Biology. Sun . "Expression, crystallization and preliminary crystallographic data analysis of filamin A repeats 14–16". United Kingdom. doi:10.1107/S1744309107006689.
@article{osti_22360291,
title = {Expression, crystallization and preliminary crystallographic data analysis of filamin A repeats 14–16},
author = {Aguda, Adeleke Halilu, E-mail: adelekeha@imcb.a-star.edu.sg and Institute of Molecular and Cell Biology and Sakwe, Amos Malle and Rask, Lars and Robinson, Robert Charles and Institute of Molecular and Cell Biology},
abstractNote = {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°.},
doi = {10.1107/S1744309107006689},
journal = {Acta Crystallographica. Section F},
number = Pt 4,
volume = 63,
place = {United Kingdom},
year = {Sun Apr 01 00:00:00 EDT 2007},
month = {Sun Apr 01 00:00:00 EDT 2007}
}