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Crystallization and preliminary crystallographic studies of Hyp‐1, a St John's wort protein implicated in the biosynthesis of hypericin

Crystallization and preliminary crystallographic studies of Hyp‐1, a St John's wort protein... According to a debated hypothesis, the biosynthesis from emodin of the medicinally important natural compound hypericin is catalyzed in St John's wort (Hypericum perforatum) by the phenolic oxidative‐coupling protein Hyp‐1. Recombinant St John's wort Hyp‐1 has been overexpressed in Escherichia coli and obtained in single‐crystal form. The crystals belong to the orthorhombic system, space group P212121, with unit‐cell parameters a = 37.5, b = 76.7, c = 119.8 Å, contain two protein molecules in the asymmetric unit and diffract X‐rays to 1.73 Å resolution. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and preliminary crystallographic studies of Hyp‐1, a St John's wort protein implicated in the biosynthesis of hypericin

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References (29)

Publisher
Wiley
Copyright
International Union of Crystallography, 2008
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309108009111
pmid
18453712
Publisher site
See Article on Publisher Site

Abstract

According to a debated hypothesis, the biosynthesis from emodin of the medicinally important natural compound hypericin is catalyzed in St John's wort (Hypericum perforatum) by the phenolic oxidative‐coupling protein Hyp‐1. Recombinant St John's wort Hyp‐1 has been overexpressed in Escherichia coli and obtained in single‐crystal form. The crystals belong to the orthorhombic system, space group P212121, with unit‐cell parameters a = 37.5, b = 76.7, c = 119.8 Å, contain two protein molecules in the asymmetric unit and diffract X‐rays to 1.73 Å resolution.

Journal

Acta Crystallographica Section FWiley

Published: May 1, 2008

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