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  Crystallization and preliminary x‐ray analysis of glucose‐fructose oxidoreductase from zymomonas mobilis

Loos, H., Ermler, U., Sprenger, G. A., & Sahm, H. (1994). Crystallization and preliminary x‐ray analysis of glucose‐fructose oxidoreductase from zymomonas mobilis. Protein Science, 3(12), 2447-2449. doi:10.1002/pro.5560031228.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0008-390D-B Version Permalink: https://hdl.handle.net/21.11116/0000-000B-A8C8-6
Genre: Journal Article

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 Creators:
Loos, Heidi1, Author
Ermler, Ulrich2, Author                 
Sprenger, Georg A.1, Author
Sahm, Hermann1, Author
Affiliations:
1Institut für Biotechnologie 1, Forschungszentrum Jülich, D‐52425 Jülich, Germany, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: crystallization; glucose‐fructose oxidoreductase; NADP(H) cofactor; X‐ray crystallography; Zymomonas mobilis
 Abstract: Glucose‐fructose oxidoreductase (E.C. 1.1.99.‐) from the ethanol‐producing Gram‐negative bacterium Zymomonas mobilis is a periplasmic, soluble enzyme that forms a homotet‐ramer of 160 kDa with one NADP(H) cofactor per subunit that is tightly, but noncovalently, bound. The enzyme was crystallized by the hanging drop vapor diffusion method using sodium citrate as precipitant. The obtained crystals belong to the space group P21212, with unit cell constants of 84.6 Å, 94.1 Å, and 117.0 Å, consistent with two monomers in the asymmetric unit. They diffract to a resolution of about 2 Å and are suitable for X‐ray structure determination.

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Language(s): eng - English
 Dates: 1994-10-121994-10-252008-12-311994-12-01
 Publication Status: Issued
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/pro.5560031228
PMID: 7756998
PMC: PMC2142752
 Degree: -

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Title: Protein Science
Source Genre: Journal
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Publ. Info: New York, N.Y. : Cambridge University Press
Pages: - Volume / Issue: 3 (12) Sequence Number: - Start / End Page: 2447 - 2449 Identifier: ISSN: 0961-8368
CoNE: https://pure.mpg.de/cone/journals/resource/954925342760