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.
rhodospirillum-rubrum
refinement
complex
crystal-structure
resolution
proton-translocating transhydrogenase
nicotinamide nucleotide transhydrogenase
nadp(h)-binding component diii
catalytic-properties
site
Författare
Christine Oswald
Chalmers
Tomas Johansson
Chalmers
Susanna Törnroth-Horsefield
Chalmers
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 4 743-745Ämneskategorier
Biokemi och molekylärbiologi
Biofysik
Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)
Kemi
DOI
10.1107/S090744490400229X