Expression, purification and preliminary X-ray diffraction studies of VERNALIZATION1208–341 from Arabidopsis thaliana

King, Gordon, Hill, Justine M., Martin, Jennifer L. and Mylne, Joshua S. (2009) Expression, purification and preliminary X-ray diffraction studies of VERNALIZATION1208–341 from Arabidopsis thaliana. Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 65 3: 291-294. doi:10.1107/S1744309109004217

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Author King, Gordon
Hill, Justine M.
Martin, Jennifer L.
Mylne, Joshua S.
Title Expression, purification and preliminary X-ray diffraction studies of VERNALIZATION1208–341 from Arabidopsis thaliana
Journal name Acta Crystallographica Section F-Structural Biology and Crystallization Communications   Check publisher's open access policy
ISSN 1744-3091
Publication date 2009-03-01
Year available 2009
Sub-type Article (original research)
DOI 10.1107/S1744309109004217
Open Access Status File (Publisher version)
Volume 65
Issue 3
Start page 291
End page 294
Total pages 4
Editor H. M. Einspahr
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell
Collection year 2010
Language eng
Subject 970106 Expanding Knowledge in the Biological Sciences
060112 Structural Biology (incl. Macromolecular Modelling)
060702 Plant Cell and Molecular Biology
060703 Plant Developmental and Reproductive Biology
C1
Formatted abstract
VERNALIZATION1 (VRN1) is required in the model plant Arabidopsis thaliana for the epigenetic suppression of the floral repressor FLC by prolonged cold treatment. Stable suppression of FLC accelerates flowering, a physiological process known as vernalization. VRN1 is a 341-residue DNA-binding protein that contains two plant-specific B3 domains (B3a and B3b), a putative nuclear localization sequence (NLS) and two putative PEST domains. VRN1208–341 includes the second B3 domain and a region upstream that is highly conserved in the VRN1 orthologues of other dicotyledonous plants. VRN1208–341 was crystallized by the hanging-drop method in 0.05 M sodium acetate pH 6.0 containing 1.0 M NaCl and 18%(w/v) PEG 3350. Preliminary X-ray diffraction data analysis revealed that the VRN1208–341 crystal diffracted to 2.1 Å and belonged to space group C2, with unit-cell parameters a = 105.2, b = 47.9, c = 61.2 Å, α = 90.0, β = 115.4, γ = 90.0°. Assuming that two molecules occupy the asymmetric unit, a Matthews coefficient of 2.05 Å3 Da−1 and a solvent content of 40.1% were calculated.
Keyword vernalization
B3 domain
DNA binding
chromatin
epigenetic suppression
Arabidopsis thaliana
Q-Index Code C1
Q-Index Status Confirmed Code

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2010 Higher Education Research Data Collection
Institute for Molecular Bioscience - Publications
 
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Created: Thu, 03 Sep 2009, 18:38:26 EST by Mr Andrew Martlew on behalf of Institute for Molecular Bioscience