| Literature DB >> 11752799 |
Mika Jormakka1, Susanna Törnroth, Jeff Abramson, Bernadette Byrne, So Iwata.
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.Entities:
Mesh：
Substances：
Year: 2001 PMID： 11752799 DOI： 10.1107/s0907444901017723
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN： 0907-4449