Purification, nanocrystallization and preliminary X-ray analysis of a C-terminal part of tropomodulin protein 1, isoform A, from Caenorhabditis elegans

Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):1106-8. doi: 10.1107/s0907444903008217. Epub 2003 May 23.

Abstract

The C-terminal part of tropomodulin protein 1, isoform A, from Caenorhabditis elegans was expressed in Escherichia coli and purified to homogeneity. Optimized from the initial nanoscreen, crystals grew to dimensions of 0.25 x 0.15 x 0.15 mm at 277 K using 28.0%(v/v) PEG 400 as the precipitant by the hanging-drop vapor-diffusion technique. A data set of 94.9% completeness was collected to a resolution of 1.98 A at 100 K using a synchrotron X-ray source (SER-CAT). The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 31.7, b = 50.6, c = 107.1 A, and contained one molecule per asymmetric unit.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Caenorhabditis elegans / metabolism*
  • Caenorhabditis elegans Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Molecular Sequence Data
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry*
  • Recombinant Proteins / genetics
  • Tropomodulin
  • X-Ray Diffraction

Substances

  • Caenorhabditis elegans Proteins
  • Recombinant Proteins
  • Tropomodulin
  • UNC-94 protein, C elegans