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Optimization of Met8p crystals through protein-storage buffer manipulation (2001)

Schubert, Heidi L. ; Raux, Evelyne ; Warren, Martin J. ; [et al.]

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 57 (2001), S. 867-869

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ISSN: 1399-0047

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: 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 Å.

Type of Medium: Electronic Resource

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

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