E Schonbrunn

Summary

Affiliation: Max-Planck-Unit for Structural Molecular Biology
Country: Germany

Publications

  1. ncbi request reprint Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin
    E Schonbrunn
    Max Planck Unit for Structural Molecular Biology, Notkestr 85, c o DESY, D 22603 Hamburg, Germany
    Structure 4:1065-75. 1996
  2. ncbi request reprint Crystallization and preliminary X-ray analysis of the single-headed and double-headed motor protein kinesin
    F Kozielski
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    J Struct Biol 119:28-34. 1997
  3. ncbi request reprint Crystallization and preliminary X-ray diffraction analysis of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae
    S Sack
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    J Struct Biol 117:73-6. 1996
  4. ncbi request reprint Crystallization of a macromolecular ring assembly of tubulin liganded with the anti-mitotic drug podophyllotoxin
    E Schonbrunn
    Max Planck Unit for Structural Molecular Biology, c o DESY, Hamburg, 22603, Germany
    J Struct Biol 128:211-5. 1999
  5. ncbi request reprint The crystal structure of dimeric kinesin and implications for microtubule-dependent motility
    F Kozielski
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    Cell 91:985-94. 1997

Detail Information

Publications5

  1. ncbi request reprint Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin
    E Schonbrunn
    Max Planck Unit for Structural Molecular Biology, Notkestr 85, c o DESY, D 22603 Hamburg, Germany
    Structure 4:1065-75. 1996
    ..EPT is of potential pharmaceutical interest because it is inhibited by the broad spectrum antibiotic fosfomycin...
  2. ncbi request reprint Crystallization and preliminary X-ray analysis of the single-headed and double-headed motor protein kinesin
    F Kozielski
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    J Struct Biol 119:28-34. 1997
    ..1 A resolution. Crystals of monomeric kinesin were also obtained with lithium sulfate as precipitant. They have cell constants of a = 71.6 A, b = 73.7 A, and c = 74.1 A and diffract up to 1.7 A resolution...
  3. ncbi request reprint Crystallization and preliminary X-ray diffraction analysis of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae
    S Sack
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    J Struct Biol 117:73-6. 1996
    ..9 A, b = 155.9 A, c = 83.8 A, beta = 91.6 degrees. Assuming two monomers per asymmetric unit, the solvent content of these crystals is 63%. Flash-frozen crystals diffract to beyond 2 A resolution...
  4. ncbi request reprint Crystallization of a macromolecular ring assembly of tubulin liganded with the anti-mitotic drug podophyllotoxin
    E Schonbrunn
    Max Planck Unit for Structural Molecular Biology, c o DESY, Hamburg, 22603, Germany
    J Struct Biol 128:211-5. 1999
    ..Thus, the use of highly homogeneous tubulin preparations should improve the diffraction quality of these crystals...
  5. ncbi request reprint The crystal structure of dimeric kinesin and implications for microtubule-dependent motility
    F Kozielski
    Max Planck Unit for Structural Molecular Biology, Hamburg, Germany
    Cell 91:985-94. 1997
    ..This arrangement is unexpected since it is not compatible with the microtubule lattice. In this arrangement, the two heads of a kinesin dimer could not have equivalent interactions with microtubules...