PMID:11752799
| Citation |
Jormakka, M, Törnroth, S, Abramson, J, Byrne, B and Iwata, S (2002) Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 58:160-2 |
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| Abstract |
A membrane-protein complex, formate dehydrogenase-N from Escherichia coli, has been purified and crystallized. This molybdenum-containing enzyme, composed of alpha, beta and gamma subunits, is the major electron donor to the nitrate respiratory chain of E. coli. The formate dehydrogenase-N crystals belong to the cubic space group P2(1)3, with unit-cell parameters a = b = c = 203 A. An asymmetric unit of the crystals is assumed to contain one formate dehydrogenase-N monomer (MW 170 kDa). One data set to 1.6 A resolution, with 342 711 independent observations (94.4% complete) and an R(merge) of 0.08, has been collected from a single crystal. This is the highest resolution data set reported for a membrane-protein complex to date. |
| Links | |
| Keywords |
Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Formate Dehydrogenases/chemistry; Formate Dehydrogenases/isolation & purification; Protein Conformation |
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