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Scientific article
English

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

Publication date2010
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.

Keywords
  • Amino Acid Motifs
  • Arabidopsis/chemistry
  • Arabidopsis Proteins/chemistry/genetics
  • Crystallization
  • Crystallography, X-Ray
  • Gene Expression
  • Nuclear Proteins/chemistry/genetics
  • Transcription Factors/chemistry/genetics
Citation (ISO format)
PETTY, Tom J. et al. Expression, crystallization and preliminary X-ray diffraction analysis of the CMM2 region of the Arabidopsis thaliana Morpheus” molecule 1 protein. In: Acta crystallographica. Section F, Structural biology and crystallization communications, 2010, vol. 66, n° Pt 8, p. 916–918. doi: 10.1107/S1744309110021068
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Article (Published version)
accessLevelRestricted
Identifiers
ISSN of the journal1744-3091
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