Subcloning, crystallization and preliminary X-ray analysis of the signal receiver domain of ETR1, an ethylene receptor from Arabidopsis thaliana.
The signal receiver domain of ETR1, an ethylene receptor from Arabidopsis thaliana, has been subcloned and expressed in E. coli and purified by affinity chromatography. Crystals of both native and a selenomethionine-substituted form of the receiver domain have been obtained. Native crystals grew in 1.6 M Li2SO4 and 0.1 M HEPES pH 7. 5 and once flash-frozen diffract to 2.1 A resolution. They belong to space group P41212 with unit-cell dimensions a = b = 48.4, c = 112.3 A.
Structural Biology Division of Lawrence Berkeley National Laboratory and Department of Chemistry, University of California, Berkeley, California 95720, USA.
A A
AA
Grantz
H J
HJ
Müller-Dieckmann
S H
SH
Kim
D017360:Arabidopsis / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D018076:DNA, Complementary / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D017434:Protein Structure, Tertiary; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011993:Recombinant Fusion Proteins / Q000737:chemistry
D018076:DNA, Complementary; D010446:Peptide Fragments; D010940:Plant Proteins; D011956:Receptors, Cell Surface; D011993:Recombinant Fusion Proteins; C083750:ethylene receptors, plant