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 .
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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.
|Uncontrolled keywords:||Buffers Crystallization Crystallography, X-Ray *Ferrochelatase Fungal Proteins/*chemistry Multienzyme Complexes/chemistry Protein Conformation Saccharomyces cerevisiae/chemistry/*metabolism *Saccharomyces cerevisiae Proteins|
|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)|
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