title: Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea.
abstract: Recombinant amylosucrase from Neisseria polysaccharea was crystallized by the vapour-diffusion procedure in the presence of polyethylene glycol 6000. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 95.7, b = 117.2, c = 62.1 A, and diffract to 1.6 A resolution. A p-chloromercuribenzene sulfonate (pcmbs) derivative has been identified and a selenomethionine-substituted protein has been produced and crystallized.
authors.affiliation: Protein Structure Group, Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark.
authors.forename: L K
authors.initials: LK
authors.lastname: Skov
authors.forename: O
authors.initials: O
authors.lastname: Mirza
authors.forename: A
authors.initials: A
authors.lastname: Henriksen
authors.forename: G
authors.initials: G
authors.lastname: Potocki de Montalk
authors.forename: M
authors.initials: M
authors.lastname: Remaud-Simeon
authors.forename: P
authors.initials: P
authors.lastname: Sarcabal
authors.forename: R M
authors.initials: RM
authors.lastname: Willemot
authors.forename: P
authors.initials: P
authors.lastname: Monsan
authors.forename: M
authors.initials: M
authors.lastname: Gajhede
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D002942:Circular Dichroism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology; D005964:Glucosyltransferases / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D009343:Neisseria / Q000201:enzymology*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; D005964:Glucosyltransferases; C019700:amylosucrase