Expression, crystallization and preliminary X-ray studies of the PDZ domain of Dishevelled protein

Authors
Khlebtsova, N Hung, LW Henderson, K Moon, R Earnest, T
Citation
N. Khlebtsova et al., Expression, crystallization and preliminary X-ray studies of the PDZ domain of Dishevelled protein, ACT CRYST D, 56, 2000, pp. 212-214
Citations number
16
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
2
Pages
212 - 214
Database
ISI
SICI code
0907-4449(200002)56:<212:ECAPXS>2.0.ZU;2-8
Abstract
Dishevelled (Dsh) protein is an important component of the Wnt signal-trans duction pathway. It has three relatively conserved domains: DIX, PDZ and DE P. The PDZ domain of the Xenopus laevis homolog of Dsh, which consists of r esidues 254-348, was overexpressed as a soluble protein in Escherichia coli , purified and crystallized. The crystals were obtained by the vapor-diffus ion method, using 1.4 M sodium formate as a precipitant. The crystals diffr acted to 2.3 Angstrom 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 Angstrom.