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Crystallization and preliminary crystallographic analysis of the NAD(H)-binding domain of Escherichia coli transhydrogenase
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- Oswald, Christine (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Johansson, Tomas (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Törnroth-Horsefield, Susanna, 1973 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- 2004
- 2004
- English.
- In: Acta Crystallographica Section D: Biological Crystallography. - 1399-0047 .- 0907-4449. ; 60:4, s. 743-745
- Journal article (peer-reviewed)
Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Keyword
- rhodospirillum-rubrum
- refinement
- complex
- crystal-structure
- resolution
- proton-translocating transhydrogenase
- nicotinamide nucleotide transhydrogenase
- nadp(h)-binding component diii
- catalytic-properties
- site
- proton-translocating transhydrogenase
- nicotinamide nucleotide transhydrogenase
- nadp(h)-binding component diii
- rhodospirillum-rubrum
- catalytic-properties
- crystal-structure
- refinement
- resolution
- complex
- site
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- ref (subject category)
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