Expression, crystallization and preliminary X-ray diffraction analysis of the CMM2 region of the Arabidopsis thaliana Morpheus' molecule 1 protein

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt 8):916-8. doi: 10.1107/S1744309110021068. Epub 2010 Jul 29.

Abstract

Of the known epigenetic control regulators found in plants, the Morpheus' molecule 1 (MOM1) protein is atypical in that the deletion of MOM1 does not affect the level of epigenetic marks controlling the transcriptional status of the genome. A short 197-amino-acid fragment of the MOM1 protein sequence can complement MOM1 deletion when coupled to a nuclear localization signal, suggesting that this region contains a functional domain that compensates for the loss of the full-length protein. Numerous constructs centred on the highly conserved MOM1 motif 2 (CMM2) present in these 197 residues have been generated and expressed in Escherichia coli. Following purification and crystallization screening, diamond-shaped single crystals were obtained that diffracted to approximately 3.2 A resolution. They belonged to the trigonal space group P3(1)21 (or P3(2)21), with unit-cell parameters a=85.64, c=292.74 A. Structure determination is ongoing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Amino Acid Motifs
  • Arabidopsis / chemistry*
  • Arabidopsis Proteins / chemistry*
  • Arabidopsis Proteins / genetics
  • Crystallization
  • Crystallography, X-Ray
  • Gene Expression
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / genetics
  • Transcription Factors / chemistry*
  • Transcription Factors / genetics

Substances

  • Arabidopsis Proteins
  • Nuclear Proteins
  • Transcription Factors
  • ATPases Associated with Diverse Cellular Activities
  • MOM protein, Arabidopsis