Crystallization and diffraction of an Lhx4-Isl2 complex

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt 2):151-3. doi: 10.1107/S1744309108043431. Epub 2009 Jan 31.

Abstract

A stable intramolecular complex comprising the LIM domains of the LIM-homeodomain protein Lhx4 tethered to a peptide region of Isl2 has been engineered, purified and crystallized. The monoclinic crystals belonged to space group P2(1), with unit-cell parameters a = 46.8, b = 88.7, c = 49.9 A, beta = 111.9 degrees, and diffracted to 2.16 A resolution.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallization
  • Homeodomain Proteins / chemistry*
  • Homeodomain Proteins / metabolism*
  • LIM-Homeodomain Proteins
  • Mice
  • Motor Neurons / chemistry
  • Motor Neurons / metabolism
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism
  • Protein Binding / physiology
  • Protein Engineering / methods
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism*
  • X-Ray Diffraction*

Substances

  • Homeodomain Proteins
  • Isl2 protein, mouse
  • LIM-Homeodomain Proteins
  • Lhx4 protein, mouse
  • Nerve Tissue Proteins
  • Transcription Factors
  • insulin gene enhancer binding protein Isl-1