Optimization of Met8p crystals through protein-storage buffer manipulation

被引：5

作者：

Schubert, HL ^{[1
]}

Raux, E

Warren, MJ

Wilson, KS

机构：

[1] Univ Utah, Dept Biochem, Salt Lake City, UT 84132 USA

[2] Univ London Queen Mary & Westfield Coll, Dept Biol Sci, London E1 4NS, England

[3] Univ York, Dept Chem, Struct Biol Lab, York YO10 5DD, N Yorkshire, England

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444901004619

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom.

引用

页码：867 / 869

页数：3