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

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.

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Genre: Journal Article
Alternative Title : Acta Crystallogr. Sect. D-Biol. Crystallogr.

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 Creators:
Abt, D. J., Author
Einsle, O., Author
Niessen, H., Author
Krieger, R., Author
Messerschmidt, A.1, 2, Author           
Schink, B., Author
Kroneck, P. M. H., Author
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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 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 Angstrom.

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Language(s): eng - English
 Dates: 2002-02
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 35337
ISI: 000173442200030
 Degree: -

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Title: Acta Crystallographica Section D - Biological Crystallography
  Alternative Title : Acta Crystallogr. Sect. D-Biol. Crystallogr.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 58 Sequence Number: - Start / End Page: 343 - 345 Identifier: ISSN: 0907-4449