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Crystallization and preliminary X-ray diffraction studies of the spinach-chloroplast thioredoxin f.

Abstract：

:Thioredoxins are low-molecular-mass proteins that function as hydrogen carriers in DNA synthesis and in the transformation of sulfur metabolites. They also act as regulatory proteins in the light-dependent enzyme activation during photosynthesis. F-type thioredoxin from spinach chloroplasts, a monomeric protein of 113 amino acid residues, has been found to specifically activate fructose-1,6-bisphosphatase and other key enzymes of CO2 assimilation. It has been crystallized in the monoclinic system, space group P2(1) with a = 30.6 A, b = 63.1 A, c = 31.6 A and beta = 110.7 degrees. The crystals are suitable for X-ray diffraction studies.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Génovésio-Taverne JC,Jetzer Y,Sauder U,Hohenester E,Hughet C,Jansonius JN,Gardet-Salvi L,Schürmann P

doi

10.1016/0022-2836(91)90488-r

subject

Has Abstract

pub_date

1991-12-05 00:00:00

pages

459-61

issue

3

eissn

0022-2836

issn

1089-8638

pii

0022-2836(91)90488-R

journal_volume

222

pub_type

杂志文章

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