Optimization of Met8p crystals through protein-storage buffer manipulation

Schubert, Heidi L. and Raux-Deery, Evelyne and Warren, Martin J. and Wilson, Keith S. (2001) Optimization of Met8p crystals through protein-storage buffer manipulation. Acta Crystallographica Section D-Biological Crystallography , 57 (6). pp. 867-869. ISSN 0907-4449 . (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1107/S0907444901004619

Abstract

Sirohaem, the prosthetic group of assimilatory sulfite and nitrite reductases, is a modified tetrapyrrole that belongs to the same fraternity of metallo-prosthetic groups as haem, chlorophyll, cobalamin and coenzyme F430 [Warren & Scott (1990), Trends Biochem Sci. 15, 486-491]. In Saccharomyces cerevisiae, the last step in the biosynthesis of sirohaem involves Met8p, a bifunctional enzyme responsible for both the NAD(+)-dependent dehydrogenation of the corrin ring and ferrochelation. Optimization of the protein storage buffer according to the results of crystallization trials resulted in a more monodisperse protein solution. Crystals were grown that diffracted to 2.1 A.

Item Type: Article
Additional information:
Uncontrolled keywords: Buffers Crystallization Crystallography, X-Ray *Ferrochelatase Fungal Proteins/*chemistry Multienzyme Complexes/chemistry Protein Conformation Saccharomyces cerevisiae/chemistry/*metabolism *Saccharomyces cerevisiae Proteins
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Martin Warren
Date Deposited: 12 Oct 2009 08:12
Last Modified: 17 Jul 2014 13:30
Resource URI: https://kar.kent.ac.uk/id/eprint/11063 (The current URI for this page, for reference purposes)
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