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  • Title: Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgX.
    Author: Weadge JT, Yip PP, Robinson H, Arnett K, Tipton PA, Howell PL.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2010 May 01; 66(Pt 5):588-91. PubMed ID: 20445266.
    Abstract:
    AlgX is a periplasmic protein required for the production of the exopolysaccharide alginate in Pseudomonas sp. and Azotobacter vinelandii. AlgX has been overexpressed and purified and diffraction-quality crystals have been grown using iterative seeding and the hanging-drop vapor-diffusion method. The crystals grew as flat plates with unit-cell parameters a = 46.4, b = 120.6, c = 86.9 A, beta = 95.7 degrees . The crystals exhibited the symmetry of space group P2(1) and diffracted to a minimum d-spacing of 2.1 A. On the basis of the Matthews coefficient (V(M) = 2.25 A(3) Da(-1)), two molecules were estimated to be present in the asymmetric unit.
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