Crystallization and preliminary X-ray crystallographic analysis of 
strictosidine synthase from Rauvolfia: the first member of a novel enzyme family

Ma, Xueyan; Koepke, Jürgen; Fritzsch, Günter; Diem, Ralf; Kutchan, Toni M.; Michel, Hartmut; Stöckigt, Joachim

doi:10.1016/j.bbapap.2004.06.013

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Crystallization and preliminary X-ray crystallographic analysis of strictosidine synthase from Rauvolfia: the first member of a novel enzyme family

Ma, X., Koepke, J., Fritzsch, G., Diem, R., Kutchan, T. M., Michel, H., et al. (2004). Crystallization and preliminary X-ray crystallographic analysis of strictosidine synthase from Rauvolfia: the first member of a novel enzyme family. Biochimica et Biophysica Acta-Proteins and Proteomics, 1702, 121-124. doi:10.1016/j.bbapap.2004.06.013.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-DACA-7 Version Permalink: https://hdl.handle.net/21.11116/0000-000B-A2ED-3

Genre: Journal Article

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Creators:
Ma, Xueyan¹, Author
Koepke, Jürgen², Author
Fritzsch, Günter², Author
Diem, Ralf², Author
Kutchan, Toni M.³, Author
Michel, Hartmut², Author
Stöckigt, Joachim¹, Author

Affiliations:
1Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes Gutenberg-University Mainz, 55099 Mainz, Germany, ou_persistent22
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290
3Leibniz Institute of Plant Biochemistry, 06120 Halle/Saale, Germany, ou_persistent22

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Free keywords: Strictosidine synthase; Crystallization; Alkaloid biosynthesis; Strictosidine synthase family

Abstract: Strictosidine synthase is a central enzyme involved in the biosynthesis of almost all plant monoterpenoid indole alkaloids. Strictosidine synthase from Rauvolfia serpentina was heterologously expressed in Escherichia coli. Crystals of the purified recombinant enzyme have been obtained by the hanging-drop technique at 303 K with potassium sodium tartrate tetrahydrate as precipitant. The crystals belong to the space group R3 with cell dimensions of a=b=150.3 A and c=122.4 A. Under cryoconditions (120 K), the crystals diffract to about 2.95 A.

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Language(s): eng - English

Dates: Submitted: 2004-04-27Accepted: 2004-06-03Published Online: 2004-08-14Date issued: 2004-10-01

Publication Status: Issued

Pages: 4

Publishing info: -

Table of Contents: -

Rev. Type: Peer

Identifiers: DOI: 10.1016/j.bbapap.2004.06.013
PMID: 15450856

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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: 1702 Sequence Number: - Start / End Page: 121 - 124 Identifier: ISSN: 1570-9639
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_5