Electron Microscopy of Human Erythrocyte Catalase: New Two-Dimensional Crystal Forms
Identifieur interne : 001692 ( Istex/Curation ); précédent : 001691; suivant : 001693Electron Microscopy of Human Erythrocyte Catalase: New Two-Dimensional Crystal Forms
Auteurs : J. R. Harris [Royaume-Uni] ; H. Engelhardt [Royaume-Uni] ; S. Volker [Royaume-Uni] ; A. Holzenburg [Royaume-Uni]Source :
- Journal of Structural Biology [ 1047-8477 ] ; 1993.
Abstract
Abstract: Using the mica-spreading "negative staining-carbon film" procedure, human erythrocyte catalase has been shown to create a number of different periodic or crystalline two-dimensional (2-D) arrays which differ in the arrangement of molecules in the repeating units and the lattice type. Digital image processing has been performed with a 2-D array which contains regularly arranged "undulating" rows of molecules and also with a 2-D crystal form, exhibiting pgg (p22121) symmetry and lattice parameters of a = 12.7 nm, b = 44 nm, and γ= 92°. The data are compared with our previous analysis of a different human erythrocyte catalase 2-D crystal, and the effect of partial-depth negative staining occurring in all the various 2-D forms is discussed.
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DOI: 10.1006/jsbi.1993.1032
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R." last="Harris">J. R. Harris</name><affiliation wicri:level="1"><mods:affiliation>Institute of Zoology II, University of Mainz, D-55099 Mainz, Germany; Department of Molecular Structural Biology, Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany; and Departments of Biochemistry and Molecular Biology, and Genetics, The University of Leeds, Leeds LS2 9JT, United Kingdom</mods:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Institute of Zoology II, University of Mainz, D-55099 Mainz, Germany; Department of Molecular Structural Biology, Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany; and Departments of Biochemistry and Molecular Biology, and Genetics, The University of Leeds, Leeds LS2 9JT</wicri:regionArea></affiliation></author><author><name sortKey="Engelhardt, H" sort="Engelhardt, H" uniqKey="Engelhardt H" first="H." last="Engelhardt">H. Engelhardt</name><affiliation wicri:level="1"><mods:affiliation>Institute of Zoology II, University of Mainz, D-55099 Mainz, Germany; Department of Molecular Structural Biology, Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany; and Departments of Biochemistry and Molecular Biology, and Genetics, The University of Leeds, Leeds LS2 9JT, United Kingdom</mods:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Institute of Zoology II, University of Mainz, D-55099 Mainz, Germany; Department of Molecular Structural Biology, Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany; and Departments of Biochemistry and Molecular Biology, and Genetics, The University of Leeds, Leeds LS2 9JT</wicri:regionArea></affiliation></author><author><name sortKey="Volker, S" sort="Volker, S" uniqKey="Volker S" first="S." last="Volker">S. 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Holzenburg</name><affiliation wicri:level="1"><mods:affiliation>Institute of Zoology II, University of Mainz, D-55099 Mainz, Germany; Department of Molecular Structural Biology, Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany; and Departments of Biochemistry and Molecular Biology, and Genetics, The University of Leeds, Leeds LS2 9JT, United Kingdom</mods:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Institute of Zoology II, University of Mainz, D-55099 Mainz, Germany; Department of Molecular Structural Biology, Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany; and Departments of Biochemistry and Molecular Biology, and Genetics, The University of Leeds, Leeds LS2 9JT</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Structural Biology</title><title level="j" type="abbrev">YJSBI</title><idno type="ISSN">1047-8477</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1993">1993</date><biblScope unit="volume">111</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="22">22</biblScope><biblScope unit="page" to="33">33</biblScope></imprint><idno type="ISSN">1047-8477</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1047-8477</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Using the mica-spreading "negative staining-carbon film" procedure, human erythrocyte catalase has been shown to create a number of different periodic or crystalline two-dimensional (2-D) arrays which differ in the arrangement of molecules in the repeating units and the lattice type. Digital image processing has been performed with a 2-D array which contains regularly arranged "undulating" rows of molecules and also with a 2-D crystal form, exhibiting pgg (p22121) symmetry and lattice parameters of a = 12.7 nm, b = 44 nm, and γ= 92°. The data are compared with our previous analysis of a different human erythrocyte catalase 2-D crystal, and the effect of partial-depth negative staining occurring in all the various 2-D forms is discussed.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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