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  Expression, purification, crystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to a unique diversity of indole alkaloid skeletons

Barleben, L., Ma, X., Koepke, J., Peng, G., Michel, H., & Stöckigt, J. (2005). Expression, purification, crystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to a unique diversity of indole alkaloid skeletons. Proteins & Proteomics, 89-92. doi:10.1016/j.bbapap.2004.09.026.

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 Creators:
Barleben, Leif1, Author
Ma, Xueyan1, Author
Koepke, Jürgen2, Author           
Peng, Guohong2, Author           
Michel, Hartmut2, Author                 
Stöckigt, Joachim1, Author
Affiliations:
1Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes Gutenberg-University Mainz, Staudinger Weg 5, D-55099 Mainz, Germany, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: Strictosidine β-d-glucosidase; Cloning and purification; Crystallization; X-ray analysis; Rauvolfia serpentina
 Abstract: Strictosidine beta-D-glucosidase, a plant enzyme initiating biosynthetic pathways to about 2000 monoterpenoid indole alkaloids with an extremely large number of various carbon skeletons, has been functionally expressed in Escherichia coli and purified to homogeneity in mg scale. Crystals suitable for X-ray analysis were found by robot-mediated screening. Using the hanging-drop technique, optimum conditions were 0.3 M ammonium sulfate, 0.1 M sodium acetate, pH 4.6 and PEG 4000 (10%) as precipitant buffer. The crystals of strictosidine glucosidase belong to the space group P4212 with unit cell dimensions of a=157.63, c=103.59 A and diffract X-rays to 2.48-A resolution

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Language(s): eng - English
 Dates: 2004-09-202004-07-202004-09-242004-10-132005-02-14
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbapap.2004.09.026
PMID: 15680242
 Degree: -

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Title: Proteins & Proteomics
Source Genre: Issue
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Publ. Info: -
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 89 - 92 Identifier: -

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Title: Biochimica et Biophysica Acta-Proteins and Proteomics
  Other : BBA-Proteins Proteomics
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1747 (1) Sequence Number: - Start / End Page: 89 - 92 Identifier: ISSN: 1570-9639
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_5