Expression, purification and preliminary X-ray diffraction studies of VERNALIZATION1 208-341 from Arabidopsis thaliana

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King, Gordon
Hill, Justine M
Martin, Jennifer L
Mylne, Joshua S
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2009
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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, [alpha] = 90.0, [beta] = 115.4, [gamma] = 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.

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Acta Crystallographica Section F: Structural Biology and Crystallization Communications

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F65

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3

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Chemical sciences

Medicinal and biomolecular chemistry not elsewhere classified

Biological sciences

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