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Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgX.

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.

SUBMITTER: Weadge JT

PROVIDER: S-EPMC2864699 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgX.

Weadge Joel T JT Yip Patrick P PP Robinson Howard H Arnett Krista K Tipton Peter A PA Howell P Lynne PL

Acta crystallographica. Section F, Structural biology and crystallization communications 20100430 Pt 5

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-s ...[more]

PMID: 20445266

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