Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Crystals of an antibody FV fragment against an integral membrane protein diffracting to 1.28 Å resolution (1995)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 21 (1995), S. 74-77 
    Details
    ISSN: 0887-3585
    Keywords: crystallization ; membrane protein ; X-ray diffraction ; atomic resolution ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The Fv fragment of a monoclonal antibody, 7E2 (IgG1, κ, murine), which is directed against the integral membrane protein cytochrome c oxidase (EC 1.9.3.1) from Paracoccus denitrificans, was cloned and produced in Escherichia coli. Crystals suitable for highresolution X-ray analysis were obtained by microdialysis under low salt conditions. The crystals belong to the orthorhombic space group P212121 with unit cell dimensions of a = 51.51 Å, b = 56.15 Å, c = 99.86 Å (1 Å = 0.1 nm) and contain one F v fragment per asymmetric unit. Using synchrotron radiation diffraction data were collected up to 1.28 Å resolution. This high resolution is very unusual for a heterodimeric protein. The crystals should open the way for refining not only the atomic positions, but also for obtaining information about internal dynamics. © 1995 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340210110
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: Tetrahydromethanopterin formyltransferase from Methanopyrus kandleri (1996)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 26 (1996), S. 118-120 
    Details
    ISSN: 0887-3585
    Keywords: Protein crystallization ; X-ray crystallography ; methanogenic Archaea ; hyperthermophilic enzymes ; halophilic enzymes ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Formylmethanofuran:tetrahydromethanopterin formyltransferase from the hyperthermophilic methanogenic Archaeon Methanopyrus kandleri (growth temperature optimum 98°C) was crystallized by vapor diffusion methods. Crystal form M obtained with 2-methyl-2,4-pentanediol as precipitant displayed the space group P21 with unit cell parameters of a = 87.0 Å, b = 75.4 Å, c = 104.7 Å, and β = 113.9° and diffracted better than 2 Å resolution. Crystal form P grown from polyethylene glycol 8000 belonged to the space group I4122 and had unit cell parameters of 157.5 Å and 242.1 Å. Diffraction data to 1.73 Å were recorded. Crystal form S which was crystallized from (NH4)2SO4in the space group I4122 with unit cell parameters of 151.3 Å and 249.5 Å diffracted at least to 2.2 Å resolution. All crystal forms probably have four molecules per asymmetric unit and are suitable for X-ray structure analysis. © 1996 Wiley-Liss, Inc.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
  • 3
    Electronic Resource
    Electronic Resource
    The Photosynthetic Reaction Center from the Purple Bacterium Rhodopseudomonas viridis (Nobel Lecture)Copyright © The Nobel Foundation 1989. - We thank the Nobel Foundation, Stockholm, for permission to print this lecture. (1989)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 28 (1989), S. 829-847 
    Details
    ISSN: 0570-0833
    Keywords: Purple bacterium ; Nobel lecture ; Photosynthesis ; X-ray structure analysis ; Proteins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In our lecture we first describe the history and methods of membrane protein crystallization, before we show how the structure of the photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis was solved. The structure of this membrane protein complex is then correlated with its function as a light-driven electron pump across the photosynthetic membrane. Finally, we draw conclusions on the structure of the photosystem II reaciton center of plants and discuss the aspects of membrane protein structure. Sections 1 (crystallization), 4 (conclusions on the structure of photosystem II reaction center and evolutionary aspects) and 5 (aspects of membrane protein structure) were presented and written by H. M., sections 2 (determination of the structure) and 3 (structure and function) by J. D. We have arranged the manuscript in this way in order to facilitate continuous reading.
    Additional Material: 23 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.198908293
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Das photosynthetische Reaktionszentrum des Purpurbakteriums Rhodopseudomonas viridis (Nobel-Vortrag)Copyright © The Nobel Foundation 1989. - Wir danken der Nobel-Stiftung, Stockholm, für die Genehmigung zum Druck einer deutschen Fassung des Vortrags. (1989)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 101 (1989), S. 872-892 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In unseren Vorträgen beschrieben wir zunächst die Geschichte und die Methoden der Kristallisation von Membranproteinen. Dann zeigen wir, wie die Struktur des photosynthetischen Reaktionszentrums aus dem Purpurbakterium Rhodopseudomonas viridis bestimmt wurde. Danach wird die Struktur dieses Membranprotein-Komplexes mit seiner Funktion als lichtegetriebene Elektronenpumpe über die photosynthetische Membran korreliert. Schließlich ziehen wir Rückschlüsse auf die Struktur des Reaktionszentrums des Photosystems II der Pflanze und diskutieren die spezifischen Gesichtspunkte der Membranprotein-Struktur. Die Abschnitte 1 (Kristallisation), 4 (Verwandtschaft mit dem Photosystem II und evolutionäre Aspekte) und 5 (Membranprotein-Struktur) wurden von H. M. im Vortrag präsentiert und verfaßt, die Abschnitte 2 (Strukturaufklärung) und 3 (Struktur und Funktion) von J. D. Wir Wählen diese Anordnung, um dem Leser das Verständnis des Zusammenhangs zu erleichtern.
    Additional Material: 23 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19891010705
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...