title: Crystallization and preliminary X-ray analysis of the molybdenum-dependent pyrogallol-phloroglucinol transhydroxylase of Pelobacter acidigallici.
abstract: Crystals of the molybdo-/iron-sulfur protein pyrogallol:phloroglucinol hydroxyltransferase (transhydroxylase; EC 1.97.1.2) from Pelobacter acidigallici were grown by vapour diffusion in an N(2)/H(2) atmosphere using polyethylene glycol as a precipitant. In this microorganism, transhydroxylase converts pyrogallol to phloroglucinol in a unique reaction without oxygen transfer from water. Growth of crystals suitable for X-ray analysis was strongly dependent on the presence of dithionite as a reducing agent. The crystals belonged to space group P1 and MAD data were collected on the iron K edge to resolutions higher than 2.5 A.
authors.affiliation: Universität Konstanz, Mathematisch-Naturwissenschaftliche Sektion, Fachbereich Biologie, Postfach M665, 78457 Konstanz, Germany.
authors.forename: Dietmar J
authors.initials: DJ
authors.lastname: Abt
authors.forename: Oliver
authors.initials: O
authors.lastname: Einsle
authors.forename: Holger
authors.initials: H
authors.lastname: Niessen
authors.forename: Robert
authors.initials: R
authors.lastname: Krieger
authors.forename: Albrecht
authors.initials: A
authors.lastname: Messerschmidt
authors.forename: Bernhard
authors.initials: B
authors.lastname: Schink
authors.forename: Peter M H
authors.initials: PM
authors.lastname: Kroneck
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D008982:Molybdenum / Q000737:chemistry / Q000378:metabolism*; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D020560:Proteobacteria / Q000201:enzymology*
chemical_list: D008982:Molybdenum; D010088:Oxidoreductases; C401266:pyrogallol hydroxyltransferase