Crystallization and preliminary X-ray diffraction studies of the spinach-chloroplast thioredoxin f.
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.
Génovésio-Taverne
J C
JC
Department of Structural Biology, University of Basel, Switzerland.
Jetzer
Y
Y
Sauder
U
U
Hohenester
E
E
Hughet
C
C
Jansonius
J N
JN
Gardet-Salvi
L
L
Schürmann
P
P
D054479:Chloroplast Thioredoxins; D002736:Chloroplasts / Q000737:chemistry*; D003461:Crystallography; D010940:Plant Proteins / Q000737:chemistry*; D010944:Plants / Q000737:chemistry*; D013879:Thioredoxins; D014961:X-Ray Diffraction
D054479:Chloroplast Thioredoxins; D010940:Plant Proteins; D013879:Thioredoxins