Expression, crystallization and preliminary X-ray studies of the PDZ domain of Dishevelled protein.
Dishevelled (Dsh) protein is an important component of the Wnt signal-transduction pathway. It has three relatively conserved domains: DIX, PDZ and DEP. The PDZ domain of the Xenopus laevis homolog of Dsh, which consists of residues 254-348, was overexpressed as a soluble protein in Escherichia coli, purified and crystallized. The crystals were obtained by the vapor-diffusion method, using 1.4 M sodium formate as a precipitant. The crystals diffracted to 2.3 A resolution. The space group was determined to be P6(1)22 or P6(5)22, with unit-cell dimensions a = b = 95.9, c = 93.9 A.
Khlebtsova
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N
Macromolecular Crystallography Facility at the Advanced Light Source, Physical Biosciences Division, MS 6-2100, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Hung
L W
LW
Henderson
K
K
Moon
R
R
Earnest
T
T
D048868:Adaptor Proteins, Signal Transducing; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D000072261:Dishevelled Proteins; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010750:Phosphoproteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D029867:Xenopus Proteins; D014982:Xenopus laevis
D048868:Adaptor Proteins, Signal Transducing; C000606586:DVL1 protein, Xenopus; D000072261:Dishevelled Proteins; D010750:Phosphoproteins; D011994:Recombinant Proteins; D029867:Xenopus Proteins