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Crystallization and preliminary X-ray analysis of the molybdenum-dependent pyrogallol-phloroglucinol transhydroxylase of Pelobacter acidigallici

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78394

Messerschmidt,  A.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Abt, D. J., Einsle, O., Niessen, H., Krieger, R., Messerschmidt, A., Schink, B., et al. (2002). Crystallization and preliminary X-ray analysis of the molybdenum-dependent pyrogallol-phloroglucinol transhydroxylase of Pelobacter acidigallici. Acta Crystallographica Section D - Biological Crystallography, 58, 343-345.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6FCC-F
Zusammenfassung
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 Angstrom.