English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Crystallization and preliminary X-ray analysis of adenylylsulfate reductase from Archaeoglobus fulgidus

Roth, A., Fritz, G., Büchert, T., Huber, H., Stetter, K. O., Ermler, U., et al. (2000). Crystallization and preliminary X-ray analysis of adenylylsulfate reductase from Archaeoglobus fulgidus. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), D56(12), 1673-1675. doi:10.1107/S0907444900013366.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Roth, Annette1, Author           
Fritz, Günther2, Author
Büchert, Thomas2, Author
Huber, Harald3, Author
Stetter, Karl Otto3, Author
Ermler, Ulrich1, Author           
Kroneck, Peter M.H., Author
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Fachbereich Biologie, Mathematisch-Naturwissenschaftliche Sektion, Universität Konstanz, Fach M665, 78457 Konstanz, Germany, ou_persistent22              
3Lehrstuhl für Mikrobiologie, Universität Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany, ou_persistent22              

Content

show
hide
Free keywords: adenylylsulfate reductase
 Abstract: A group of anaerobic microorganisms use sulfate as the terminal electron acceptor for energy conservation. The process of sulfate reduction involves several enzymatic steps. One of them is the conversion of adenylyl sulfate (adenosine-5′-phosphosulfate) to sulfite, catalyzed by adenylylsulfate reductase. This enzyme is composed of a FAD-containing α-subunit and a β-subunit harbouring two [4Fe–4S] clusters. Adenylylsulfate reductase was isolated from Archaeoglobus fulgidus under anaerobic conditions and crystallized using the hanging-drop vapour-diffusion method using PEG 4000 as precipitant. The crystals grew in space group P212121, with unit-cell parameters a = 72.4, b = 113.2, c = 194.0 Å. The asymmetric unit probably contains two αβ units. The crystals diffract beyond 2 Å resolution and are suitable for X-ray structure analysis.

Details

show
hide
Language(s): eng - English
 Dates: 2000-05-312000-09-272000-12
 Publication Status: Issued
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S0907444900013366
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
  Other : Acta Crystallogr D
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: [Copenhagen, Denmark : Published for the International Union of Crystallography by Munksgaard]
Pages: - Volume / Issue: D56 (12) Sequence Number: - Start / End Page: 1673 - 1675 Identifier: ISSN: 0907-4449
CoNE: https://pure.mpg.de/cone/journals/resource/954925562619