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

J C Génovésio-Taverne; Y Jetzer; U Sauder; E Hohenester; C Hughet; J N Jansonius; L Gardet-Salvi; P Schürmann

doi:10.1016/0022-2836(91)90488-r

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

J Mol Biol. 1991 Dec 5;222(3):459-61. doi: 10.1016/0022-2836(91)90488-r.

Authors

J C Génovésio-Taverne¹, Y Jetzer, U Sauder, E Hohenester, C Hughet, J N Jansonius, L Gardet-Salvi, P Schürmann

Affiliation

¹ Department of Structural Biology, University of Basel, Switzerland.

PMID: 1748990
DOI: 10.1016/0022-2836(91)90488-r

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Chloroplast Thioredoxins
Chloroplasts / chemistry*
Crystallography*
Plant Proteins / chemistry*
Plants / chemistry*
Thioredoxins*
X-Ray Diffraction

Substances

Chloroplast Thioredoxins
Plant Proteins
Thioredoxins