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Purification, crystallization and preliminary crystallographic analysis of Arabidopsis thaliana imidazoleglycerol‐phosphate dehydratase

Purification, crystallization and preliminary crystallographic analysis of Arabidopsis thaliana... Imidazoleglycerol‐phosphate dehydratase catalyses the sixth step of the histidine‐biosynthesis pathway in plants and microorganisms and has been identified as a possible target for the development of novel herbicides. Arabidopsis thaliana IGPD has been cloned and overexpressed in Escherichia coli, purified and subsequently crystallized in the presence of manganese. Under these conditions, the inactive trimeric form of the metal‐free enzyme is assembled into a fully active species consisting of a 24‐mer exhibiting 432 symmetry. X‐ray diffraction data have been collected to 3.0 Å resolution from a single crystal at 293 K. The crystal belongs to space group R3, with approximate unit‐cell parameters a = b = 157.9, c = 480.0 Å, α = β = 90, γ = 120° and with either 16 or 24 subunits in the asymmetric unit. A full structure determination is under way in order to provide insights into the mode of subunit assembly and to initiate a programme of rational herbicide design. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Purification, crystallization and preliminary crystallographic analysis of Arabidopsis thaliana imidazoleglycerol‐phosphate dehydratase

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References (10)

Publisher
Wiley
Copyright
Copyright © 2005 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309105022451
pmid
16511155
Publisher site
See Article on Publisher Site

Abstract

Imidazoleglycerol‐phosphate dehydratase catalyses the sixth step of the histidine‐biosynthesis pathway in plants and microorganisms and has been identified as a possible target for the development of novel herbicides. Arabidopsis thaliana IGPD has been cloned and overexpressed in Escherichia coli, purified and subsequently crystallized in the presence of manganese. Under these conditions, the inactive trimeric form of the metal‐free enzyme is assembled into a fully active species consisting of a 24‐mer exhibiting 432 symmetry. X‐ray diffraction data have been collected to 3.0 Å resolution from a single crystal at 293 K. The crystal belongs to space group R3, with approximate unit‐cell parameters a = b = 157.9, c = 480.0 Å, α = β = 90, γ = 120° and with either 16 or 24 subunits in the asymmetric unit. A full structure determination is under way in order to provide insights into the mode of subunit assembly and to initiate a programme of rational herbicide design.

Journal

Acta Crystallographica Section FWiley

Published: Aug 1, 2005

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