title: 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.
authors.affiliation: Program in Molecular Structure and Function, The Hospital for Sick Children, 555 University Avenue, Toronto, Ontario M5G 1X8, Canada.
authors.forename: Joel T
authors.initials: JT
authors.lastname: Weadge
authors.forename: Patrick P
authors.initials: PP
authors.lastname: Yip
authors.forename: Howard
authors.initials: H
authors.lastname: Robinson
authors.forename: Krista
authors.initials: K
authors.lastname: Arnett
authors.forename: Peter A
authors.initials: PA
authors.lastname: Tipton
authors.forename: P Lynne
authors.initials: PL
authors.lastname: Howell
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D011550:Pseudomonas aeruginosa / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins
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