Crystallization and preliminary crystallographic analysis of the NAD(H)-binding domain of Escherichia coli transhydrogenase
Artikel i vetenskaplig tidskrift, 2004

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 Å, α = 67.5, β = 80.8, γ = 81.5°. X-ray diffraction data were collected to 1.9 Å resolution using synchrotron radiation. The crystals contain one dimer of transhydrogenase domain I per asymmetric unit. © 2004 International Union of Crystallography. Printed in Denmark - all rights reserved.

catalytic-properties

proton-translocating transhydrogenase

site

resolution

rhodospirillum-rubrum

nadp(h)-binding component diii

nicotinamide nucleotide transhydrogenase

complex

crystal-structure

refinement

Författare

Christine Oswald

Chalmers University of Technology

Tomas Johansson

Chalmers University of Technology

Susanna Törnroth-Horsefield

Chalmers University of Technology

M. Ökvist

Göteborgs universitet

Ute Krengel

Chalmers, Institutionen för kemi och biovetenskap

Acta Crystallographica Section D: Biological Crystallography

0907-4449 (ISSN) 1399-0047 (eISSN)

Vol. 60 743-745

Ämneskategorier

Biokemi och molekylärbiologi

Biofysik

Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

Kemi

DOI

10.1107/S090744490400229X