Crystallization and preliminary X-ray analysis of the molybdenum-dependent pyrogallol-phloroglucinol transhydroxylase of Pelobacter acidigallici.
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.
Abt
Dietmar J
DJ
Universität Konstanz, Mathematisch-Naturwissenschaftliche Sektion, Fachbereich Biologie, Postfach M665, 78457 Konstanz, Germany.
Einsle
Oliver
O
Niessen
Holger
H
Krieger
Robert
R
Messerschmidt
Albrecht
A
Schink
Bernhard
B
Kroneck
Peter M H
PM
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*
D008982:Molybdenum; D010088:Oxidoreductases; C401266:pyrogallol hydroxyltransferase