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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt 4):291-3. doi: 10.1107/S1744309107006689. Epub 2007 Mar 12.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Cloning, Molecular
  • Contractile Proteins / chemistry*
  • Contractile Proteins / genetics
  • Crystallization
  • Crystallography, X-Ray
  • DNA Primers
  • DNA, Complementary
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / genetics
  • Filamins
  • Humans
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / genetics
  • Protein Conformation

Substances

  • Contractile Proteins
  • DNA Primers
  • DNA, Complementary
  • Filamins
  • Microfilament Proteins