title: Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli.
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.
authors.affiliation: Division of Biomedical Sciences, Imperial College, London SW7 2AZ, England.
authors.forename: Mika
authors.initials: M
authors.lastname: Jormakka
authors.forename: Susanna
authors.initials: S
authors.lastname: Törnroth
authors.forename: Jeff
authors.initials: J
authors.lastname: Abramson
authors.forename: Bernadette
authors.initials: B
authors.lastname: Byrne
authors.forename: So
authors.initials: S
authors.lastname: Iwata
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D005560:Formate Dehydrogenases / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation
chemical_list: D005560:Formate Dehydrogenases