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Crystallization and...
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Oswald, ChristineChalmers tekniska högskola,Chalmers University of Technology
(author)
Crystallization and preliminary crystallographic analysis of the NAD(H)-binding domain of Escherichia coli transhydrogenase
- Article/chapterEnglish2004
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LIBRIS-ID:oai:research.chalmers.se:79ebf49e-5820-40b9-89e0-bb9320c38716
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https://doi.org/10.1107/S090744490400229XDOI
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https://research.chalmers.se/publication/79948URI
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https://gup.ub.gu.se/publication/79948URI
Supplementary language notes
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Language:English
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Summary in:English
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Subject category:art swepub-publicationtype
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Subject category:ref swepub-contenttype
Notes
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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.
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Johansson, TomasChalmers tekniska högskola,Chalmers University of Technology
(author)
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Törnroth-Horsefield, Susanna,1973Chalmers tekniska högskola,Chalmers University of Technology(Swepub:gu)xtorsu
(author)
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Ökvist, M.Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry
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Krengel, Ute,1964Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)mbtuk
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Chalmers tekniska högskolaInstitutionen för kemi
(creator_code:org_t)
Related titles
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In:Acta Crystallographica Section D: Biological Crystallography60:4, s. 743-7451399-00470907-4449
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