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

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Published in Acta Crystallographica. F, Structural Biology and Crystallization Communications. 2010, vol. 66, no. Pt 8, p. 916-8
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 MotifsArabidopsis/chemistryArabidopsis Proteins/chemistry/geneticsCrystallizationCrystallography, X-RayGene ExpressionNuclear Proteins/chemistry/geneticsTranscription Factors/chemistry/genetics
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PMID: 20693667
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PETTY II, Thomas John 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. F, Structural Biology and Crystallization Communications, 2010, vol. 66, n° Pt 8, p. 916-8. https://archive-ouverte.unige.ch/unige:19599

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Deposited on : 2012-04-23

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