Expression, purification and X-ray crystallographic analysis of thioredoxin from Streptomyces coelicolor.

Thioredoxins are ubiquitous proteins that serve as reducing agents and general protein disulfide reductases. In turn, they are reduced by electrons obtained from the NADPH-containing thioredoxin reductase. Thioredoxins have been isolated and characterized from a large number of organisms.

Crystallization and preliminary diffraction studies of malate dehydrogenase from Streptomyces aureofaciens.

Purified malate dehydrogenase (MDH) of Streptomyces aureofaciens was crystallized either in the absence or in the presence of NADH or NADPH coenzymes by hanging-drop vapour-diffusion method. An X-ray study has shown, that MDH crystals belong to space group C222(1) with unit-cell parameters a = 53.2 A, b = 104.

[N-(Carboxylatomethyl)aspartato(3-)](ethylenediamine)cobalt(III) trihydrate.

The mononuclear title complex, [Co(C(6)H(6)NO(6))(C(2)H(8)N(2))].3H(2)O, contains an octahedrally coordinated Co(III) atom. The N-(carboxymethyl)aspartate moiety is coordinated as a tetradentate ligand, providing an OONO-donor set and forming two trans five-membered chelate rings and one six-membered chelate ring.