PMID:2666412
| Citation |
Kuriyan, J, Wong, L, Russel, M and Model, P (1989) Crystallization and preliminary x-ray characterization of thioredoxin reductase from Escherichia coli. J. Biol. Chem. 264:12752-3 |
|---|---|
| Abstract |
Single crystals of thioredoxin reductase, suitable for x-ray diffraction studies, have been obtained at room temperature by vapor diffusion of 10-20 mg/ml protein solution against 35% polyethylene glycol containing 200 mM ammonium sulfate. Good quality crystals appear spontaneously only from a protein solution that had been stored for more than a year at 4 degrees C, although large single crystals are reproducibly obtained from fresh protein solutions by micro-seeding. The space group is P6(3)22 (a = b = 123.8 A, c = 81.6 A), with one monomer of the enzyme (34.5 kDa) in the crystallographic asymmetric unit. The crystals are well ordered and diffract to beyond 2 A resolution. |
| Links | |
| Keywords |
Crystallization; Escherichia coli/enzymology; NADH, NADPH Oxidoreductases; Protein Conformation; Thioredoxin-Disulfide Reductase; X-Ray Diffraction |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.