Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli

Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):160-2. doi: 10.1107/s0907444901017723. Epub 2001 Dec 21.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Formate Dehydrogenases / chemistry*
  • Formate Dehydrogenases / isolation & purification
  • Protein Conformation

Substances

  • Formate Dehydrogenases