Optimization of Met8p crystals through protein-storage buffer manipulation

Schubert, H.L. and Raux, E. and Warren, M.J. and Wilson, K.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 available from this repository)

The full text of this publication is not available from this repository. (Contact us about this Publication)
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: 14 Jan 2010 14:42
Resource URI: http://kar.kent.ac.uk/id/eprint/11063 (The current URI for this page, for reference purposes)
  • Depositors only (login required):