PMID:15039572
| Citation |
Oswald, C, Johansson, T, Törnroth, S, Okvist, M and Krengel, U (2004) Crystallization and preliminary crystallographic analysis of the NAD(H)-binding domain of Escherichia coli transhydrogenase. Acta Crystallogr. D Biol. Crystallogr. 60:743-5 |
|---|---|
| Abstract |
Transhydrogenase is a proton-pumping membrane protein that is required for the cellular regeneration of NADPH. The NAD(H)-binding domain (domain I) of transhydrogenase from Escherichia coli was crystallized using the hanging-drop vapour-diffusion technique at room temperature. The crystals, which were grown from PEG 4000 and ammonium acetate in citrate buffer, belong to the triclinic space group P1, with unit-cell parameters a = 38.8, b = 66.8, c = 76.4 A, alpha = 67.5, beta = 80.8, gamma = 81.5 degrees. X-ray diffraction data were collected to 1.9 A resolution using synchrotron radiation. The crystals contain one dimer of transhydrogenase domain I per asymmetric unit. |
| Links |
PubMed Online version:10.1107/S090744490400229X |
| Keywords |
Binding Sites; Cloning, Molecular; Crystallization; Crystallography, X-Ray; Escherichia coli Proteins/chemistry; NAD/chemistry; NADP Transhydrogenases/chemistry |
| 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.