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  • 1
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of human muscle creatine kinase (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 669-670 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Creatine kinase is a key enzyme in the energy homeostasis of cells and tissues with high and fluctuating energy demands. Human muscle MM creatine kinase is a dimeric protein with a molecular weight of \sim43 kDa for each subunit. It has been crystallized by the hanging-drop vapor-diffusion method using 2-methyl-2,4-pentanediol as precipitant. The crystals belong to the enantiomorphous space group P6_222 or P6_422 with cell parameters of a=b=89.11 and c=403.97 Å. The asymmetric unit of the crystal contains two subunits. A data set at 3.3 Å resolution has been collected using synchrotron radiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998011044
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Structure of agkistrodotoxin in an orthorhombic crystal form with six molecules per asymmetric unit (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1986-1996 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The structure of agkistrodotoxin crystallized under basic conditions has been determined at 2.8 Å resolution by the molecular-replacement technique and refined to a crystallographic R factor of 0.194 and a free R factor of 0.260 with good stereochemistry. The molecular packing in the crystal differs from other PLA2s. The six molecules in the asymmetric unit form three dimers linked by Ca2+ ions in a near-perfect six-ligand octahedral coordinating system. Extensive intermolecular hydrophobic interactions occur at the interfacial recognition site of each neurotoxin molecule, which provides an insight into phospholipase A2–membrane interactions. This hydrophobic interaction-induced molecular association along the interfacial recognition site suggests a self-protection mechanism of agkistrodotoxin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999012603
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Structure of human muscle creatine kinase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1196-1200 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structure of human muscle creatine kinase has been determined by the molecular-replacement method and refined at 3.5 Å resolution. The structures of both the monomer and the dimer closely resemble those of the other known structures in the creatine kinase family. Two types of dimers, one with a non-crystallographic twofold symmetry axis and the other with a crystallographic twofold symmetry axis, were found to occur simultaneously in the crystal. These dimers form an infinite `double-helix'-like structure along an unusual long crystallographic 31 axis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901007703
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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