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  • Title: Expression, refolding, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgE.
    Author: Whitney JC, Neculai AM, Ohman DE, Howell PL.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2009 May 01; 65(Pt 5):463-6. PubMed ID: 19407377.
    Abstract:
    AlgE is an outer membrane protein present in alginate-producing (mucoid) Pseudomonas aeruginosa. AlgE has been overexpressed in insoluble inclusion bodies, purified under denaturing conditions and refolded in a buffer containing decyl beta-D-maltopyranoside. Purified refolded AlgE was detergent-exchanged into n-octyl tetraoxyethylene and diffraction-quality crystals were grown using the hanging-drop vapor-diffusion method. The crystals grew as small hexagons with unit-cell parameters a = 98.8, b = 156.8, c = 90.4 A, alpha = beta = gamma = 90.0 degrees . The crystals exhibited the symmetry of space group C222 and diffracted to a minimum d-spacing of 3.0 A. On the basis of the Matthews coefficient (V(M) = 3.28 A(3) Da(-1)), one molecule is estimated to be present in the asymmetric unit.
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