Wolfgang Baumeister

Summary

Country: Germany

Publications

  1. ncbi request reprint Correlative microscopy: bridging the gap between fluorescence light microscopy and cryo-electron tomography
    Anna Sartori
    Max Planck Institute of Biochemistry, Department of Molecular Structural Biology, Am Klopferspitz 18, 82152 Martinsried, Germany
    J Struct Biol 160:135-45. 2007
  2. pmc 3D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography
    Daniela Nicastro
    Abteilung Molekulare Strukturbiologie, Max Planck Institut fur Biochemie, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 102:15889-94. 2005
  3. ncbi request reprint Localization of protein complexes by pattern recognition
    Christoph Best
    Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Methods Cell Biol 79:615-38. 2007
  4. pmc Three-dimensional architecture of murine rod outer segments determined by cryoelectron tomography
    Stephan Nickell
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    J Cell Biol 177:917-25. 2007
  5. pmc Structure of hibernating ribosomes studied by cryoelectron tomography in vitro and in situ
    Julio O Ortiz
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
    J Cell Biol 190:613-21. 2010
  6. pmc Quantitative analysis of the native presynaptic cytomatrix by cryoelectron tomography
    Rubén Fernández-Busnadiego
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    J Cell Biol 188:145-56. 2010
  7. pmc Cryo-electron tomography: the challenge of doing structural biology in situ
    Vladan Lucic
    Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    J Cell Biol 202:407-19. 2013
  8. pmc Cryo-electron tomography of cells: connecting structure and function
    Vladan Lucic
    Max Planck Institute for Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany
    Histochem Cell Biol 130:185-96. 2008
  9. pmc Geometric constrains for detecting short actin filaments by cryogenic electron tomography
    Mikhail Kudryashev
    Parasitology, Department of Infectious Diseases, University of Heidelberg Medical School, Im Neuenheimer Feld 324, D 69120 Heidelberg, Germany
    PMC Biophys 3:6. 2010
  10. pmc The regulatory complex of Drosophila melanogaster 26S proteasomes. Subunit composition and localization of a deubiquitylating enzyme
    H Hölzl
    Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    J Cell Biol 150:119-30. 2000

Detail Information

Publications139 found, 100 shown here

  1. ncbi request reprint Correlative microscopy: bridging the gap between fluorescence light microscopy and cryo-electron tomography
    Anna Sartori
    Max Planck Institute of Biochemistry, Department of Molecular Structural Biology, Am Klopferspitz 18, 82152 Martinsried, Germany
    J Struct Biol 160:135-45. 2007
    ..We have successfully tested the experimental setup and the whole procedure with two types of adherent fluorescently labelled cells, a neuronal cell line and keratinocytes, both grown directly on EM grids...
  2. pmc 3D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography
    Daniela Nicastro
    Abteilung Molekulare Strukturbiologie, Max Planck Institut fur Biochemie, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 102:15889-94. 2005
    ..Cryo-electron tomography has proven to be a powerful technique for helping us understand the relationships between flagellar structure and function and the design of macromolecular machines in situ...
  3. ncbi request reprint Localization of protein complexes by pattern recognition
    Christoph Best
    Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Methods Cell Biol 79:615-38. 2007
  4. pmc Three-dimensional architecture of murine rod outer segments determined by cryoelectron tomography
    Stephan Nickell
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    J Cell Biol 177:917-25. 2007
    ..Spacers were found distributed throughout the discs, including regions that are distant from the rim region of discs...
  5. pmc Structure of hibernating ribosomes studied by cryoelectron tomography in vitro and in situ
    Julio O Ortiz
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
    J Cell Biol 190:613-21. 2010
    ..In situ studies with intact E. coli cells allowed us to demonstrate that 100S ribosomes do exist in vivo and represent an easily reversible state of quiescence; they readily vanish when the growth medium is replenished...
  6. pmc Quantitative analysis of the native presynaptic cytomatrix by cryoelectron tomography
    Rubén Fernández-Busnadiego
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    J Cell Biol 188:145-56. 2010
    ....
  7. pmc Cryo-electron tomography: the challenge of doing structural biology in situ
    Vladan Lucic
    Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    J Cell Biol 202:407-19. 2013
    ..These new techniques have enabled the extraction of high fidelity structural information and are beginning to reveal the macromolecular organization of unperturbed cellular environments. ..
  8. pmc Cryo-electron tomography of cells: connecting structure and function
    Vladan Lucic
    Max Planck Institute for Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany
    Histochem Cell Biol 130:185-96. 2008
    ....
  9. pmc Geometric constrains for detecting short actin filaments by cryogenic electron tomography
    Mikhail Kudryashev
    Parasitology, Department of Infectious Diseases, University of Heidelberg Medical School, Im Neuenheimer Feld 324, D 69120 Heidelberg, Germany
    PMC Biophys 3:6. 2010
    ..In silico simulations of EM data collection and tomographic reconstruction identify the limits in revealing the filaments due to their length, concentration and orientation.PACS Codes: 87.64.Ee...
  10. pmc The regulatory complex of Drosophila melanogaster 26S proteasomes. Subunit composition and localization of a deubiquitylating enzyme
    H Hölzl
    Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    J Cell Biol 150:119-30. 2000
    ..This value is in good agreement with the summed masses of the 18 identified RC subunits (932 kD), indicating that the number of subunits is complete...
  11. ncbi request reprint Mapping molecular landscapes inside cells
    Wolfgang Baumeister
    Department of Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Biol Chem 385:865-72. 2004
    ..Tomograms with molecular resolution are essentially images of the cellular proteome and, in conjunction with advanced pattern recognition techniques, they can be used to map the molecular landscape inside organelles and cells...
  12. ncbi request reprint Electron tomography: towards visualizing the molecular organization of the cytoplasm
    Wolfgang Baumeister
    Department of Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Curr Opin Struct Biol 12:679-84. 2002
    ..This opens up exciting perspectives for visualizing the molecular organization of the cytoplasm...
  13. ncbi request reprint Macromolecular electron microscopy in the era of structural genomics
    W Baumeister
    Dept of Molecular Structural Biology, Max Planck Institut fur Biochemie, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Trends Biochem Sci 25:624-31. 2000
    ..Moreover, cryo-EM can be combined in several ways with X-ray diffraction to enhance the resolution of cryo-EM and the applicability of crystallography. Electron tomography holds promise for visualizing machines at work inside cells...
  14. ncbi request reprint From proteomic inventory to architecture
    Wolfgang Baumeister
    Department of Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    FEBS Lett 579:933-7. 2005
    ....
  15. pmc A voyage to the inner space of cells
    Wolfgang Baumeister
    Department of Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Protein Sci 14:257-69. 2005
  16. pmc The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together
    Ganesh Ramnath Pathare
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 109:149-54. 2012
    ..The structure suggests that Rpn6 has a pivotal role in stabilizing the otherwise weak interaction between the CP and the RP...
  17. pmc Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation
    Paweł Sledź
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 110:7264-9. 2013
    ..We postulate that ATP hydrolysis by the regulatory particle ATPase (Rpt) 5 subunit initiates a cascade of conformational changes, leading to pulling of the substrate, which is primarily executed by Rpt1, Rpt2, and Rpt6...
  18. ncbi request reprint Size matters for the tripeptidylpeptidase II complex from Drosophila: The 6-MDa spindle form stabilizes the activated state
    Gönül Seyit
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Biol Chem 281:25723-33. 2006
    ..The strands inherently heterogeneous in length are thus locked into a discrete oligomeric state. Our data indicate that the unique spindle form of the holo-complex represents an assembly motif stabilizing a highly active state...
  19. doi request reprint The structure of human tripeptidyl peptidase II as determined by a hybrid approach
    Anne Marie Schönegge
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Structure 20:593-603. 2012
    ..Analyses of the resulting hybrid structure of the HsTPPII holocomplex provide new insights into the mechanism of maturation and activation...
  20. pmc Focused ion beam micromachining of eukaryotic cells for cryoelectron tomography
    Alexander Rigort
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 109:4449-54. 2012
    ..We illustrate the quality of sample preservation with a structure of the nuclear pore complex obtained from a single tomogram...
  21. ncbi request reprint Tricorn protease--the core of a modular proteolytic system
    T Tamura
    Max Planck Institute for Biochemistry, D 82152 Martinsried, Germany
    Science 274:1385-9. 1996
    ..Tricorn protease appeared to act as the core of a proteolytic system; when it interacted with several smaller proteins, it displayed multicatalytic activities...
  22. ncbi request reprint VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase
    Alexandra Gerega
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    J Biol Chem 280:42856-62. 2005
    ..In contrast, two neighboring residues in the D2 section of the pore had to be exchanged simultaneously, to achieve a drastic inhibition of GFP unfolding...
  23. pmc Insights into the molecular architecture of the 26S proteasome
    Stephan Nickell
    Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 106:11943-7. 2009
    ..In addition, a variable mass near the mouth of the ATPase ring has been identified as Rpn10, a multiubiquitin receptor, by correlating the electron microscopy data with quantitative mass spectrometry...
  24. pmc Near-atomic resolution structural model of the yeast 26S proteasome
    Florian Beck
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 109:14870-5. 2012
    ..Together with the C-terminal helices of the six PCI-domain subunits they form a very large coiled-coil bundle, which appears to serve as a flexible anchoring device for all the lid subunits...
  25. ncbi request reprint Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography
    Ohad Medalia
    Max Planck Institute for Biochemistry, D 82152 Martinsried, Germany
    Science 298:1209-13. 2002
    ..At a resolution of 5 to 6 nanometers, single macromolecules with distinct shapes, such as the 26S proteasome, can be identified in an unperturbed cellular environment...
  26. ncbi request reprint Mapping 70S ribosomes in intact cells by cryoelectron tomography and pattern recognition
    Julio O Ortiz
    Max Planck Institute of Biochemistry, Department of Structural Biology, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Struct Biol 156:334-41. 2006
    ..This study represents a first step towards generating a more comprehensive cellular atlas of macromolecular complexes...
  27. pmc Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11
    Ganesh Ramnath Pathare
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 111:2984-9. 2014
    ..The narrow space around the Rpn11 active site at the entrance to the ATPase ring pore is likely to prevent erroneous deubiquitylation of folded proteins. ..
  28. ncbi request reprint Organization of actin networks in intact filopodia
    Ohad Medalia
    Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
    Curr Biol 17:79-84. 2007
    ..We hypothesize that growth of the highly dynamic filopodia of Dictyostelium is accompanied by repetitive nucleation of actin polymerization at the filopod tip, followed by the rearrangement of filaments within the shaft...
  29. ncbi request reprint Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution
    J Lowe
    Max Planck Institut fur Biochemie, Abteilung für Strukturforschung, Martinsried, Germany
    Science 268:533-9. 1995
    ..The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism...
  30. pmc Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome
    Pia Unverdorben
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 111:5544-9. 2014
    ..Based on the conformational ensemble of the 26S proteasome in solution, we propose a mechanistic model for substrate recognition, commitment, deubiquitylation, and translocation into the core particle. ..
  31. doi request reprint Unraveling the structure of membrane proteins in situ by transfer function corrected cryo-electron tomography
    Matthias Eibauer
    Max Planck Institut fur Biochemie, Martinsried, Germany
    J Struct Biol 180:488-96. 2012
    ..We were able to demonstrate that structural information up to a resolution of 16.8Å can be recovered using our CTF correction approach, whereas the uncorrected 3D map had a resolution of only 26.2Å...
  32. pmc Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy
    Eri Sakata
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried 82152, Germany
    Proc Natl Acad Sci U S A 109:1479-84. 2012
    ..On the basis of the mutual positions of Rpn10 and Rpn13, we propose a model for polyubiquitin binding to the 26S proteasome...
  33. ncbi request reprint Automated cryoelectron microscopy of "single particles" applied to the 26S proteasome
    Stephan Nickell
    Max Planck Institute of Biochemistry, Department of Structural Biology, Am Klopferspitz 18, D 82152 Martinsried, Germany
    FEBS Lett 581:2751-6. 2007
    ..The application of this procedure to the 26S proteasome from Drosophila has allowed us to determine the three-dimensional structure of the complex to a resolution of 2.9 nm and the prospects for further improvements are good...
  34. ncbi request reprint Structural studies by electron tomography: from cells to molecules
    Vladan Lucic
    Department of Structural Biology, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    Annu Rev Biochem 74:833-65. 2005
    ....
  35. ncbi request reprint Pyrodictium cannulae enter the periplasmic space but do not enter the cytoplasm, as revealed by cryo-electron tomography
    Stephan Nickell
    Max Planck Institut fur Biochemie, Abteilung Molekulare Strukturbiologie, D 82152 Martinsried, Germany
    J Struct Biol 141:34-42. 2003
    ..The implications of these data for possible functions of the cannulae are discussed...
  36. ncbi request reprint Nuclear pore complex structure and dynamics revealed by cryoelectron tomography
    Martin Beck
    Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    Science 306:1387-90. 2004
    ..Changes in the position of the CP/T were accompanied by structural rearrangements in the NPC scaffold...
  37. ncbi request reprint Cryo-electron tomography reveals the cytoskeletal structure of Spiroplasma melliferum
    Julia Kürner
    Department of Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Science 307:436-8. 2005
    ..On the basis of our structural data, we could model the motility modes of these cells and explain how helical Mollicutes can propel themselves by means of coordinated length changes of their cytoskeletal ribbons...
  38. ncbi request reprint Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    Martin Beck
    Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    Nature 449:611-5. 2007
    ..Finally, we have performed single-molecule Monte Carlo simulations of nuclear import to interpret the experimentally observed cargo distribution in the light of existing models for nuclear import...
  39. ncbi request reprint Characterization of ARC, a divergent member of the AAA ATPase family from Rhodococcus erythropolis
    S Wolf
    Max Planck Institut fur Biochemie, Am Klopferspitz 18a, Martinsried, D 82152, Germany
    J Mol Biol 277:13-25. 1998
    ..Two-dimensional crystals grown on lipid monolayers yielded images of the ATPase molecules in "end-on" orientation at 1.9 nm resolution...
  40. ncbi request reprint Multiscale imaging of neurons grown in culture: from light microscopy to cryo-electron tomography
    Vladan Lucic
    Max Planck Institute for Biochemistry, Department of Structural Biology, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Struct Biol 160:146-56. 2007
    ..The correlation method presented here can be expected to provide new insights into the structure-function relationship of supramolecular organization in neurons...
  41. pmc An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome
    Friedrich Förster
    Department of Structural Biology, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    Biochem Biophys Res Commun 388:228-33. 2009
    ..Furthermore, the atomic CP-AAA-ATPase model suggests that the assembly chaperone Nas6 facilitates CP-RP association by enhancing the shape complementarity between Rpt3 and its binding CP alpha subunits partners...
  42. pmc Cryoelectron tomography reveals periodic material at the inner side of subpellicular microtubules in apicomplexan parasites
    Marek Cyrklaff
    Department of Molecular Structural Biology, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany
    J Exp Med 204:1281-7. 2007
    ..Microtubules from extracted sporozoites and Toxoplasma gondii tachyzoites showed a similar density distribution, suggesting that the putative protein is conserved among Apicomplexa and serves to stabilize microtubules...
  43. doi request reprint Localization of the regulatory particle subunit Sem1 in the 26S proteasome
    Stefan Bohn
    Max Planck Institute of Biochemistry, Department of Molecular Structural Biology, D 82152 Martinsried, Germany
    Biochem Biophys Res Commun 435:250-4. 2013
    ..Our structural studies indicate that Sem1 can assume different conformations in different contexts, which supports the idea that Sem1 functions as a molecular glue stabilizing the Rpn3/Rpn7 heterodimer...
  44. pmc Cryo-electron tomography reveals a critical role of RIM1α in synaptic vesicle tethering
    Rubén Fernández-Busnadiego
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    J Cell Biol 201:725-40. 2013
    ....
  45. doi request reprint Molecular ruler of tripeptidylpeptidase II: mechanistic principle of exopeptidase selectivity
    Jürgen Peters
    Max Planck Institute of Biochemistry, Department of Molecular Structural Biology, Am Klopferspitz 18, 82152 Martinsried, Germany
    Biochem Biophys Res Commun 414:209-14. 2011
    ..However, the lacking alignment of the substrate by the double-Glu motif causes the endopeptidolytic K(cat)/K(M) of TPPII to be very low...
  46. ncbi request reprint Structural analysis of the 26S proteasome by cryoelectron tomography
    Stephan Nickell
    Max Planck Institute of Biochemistry, Department of Structural Biology, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Biochem Biophys Res Commun 353:115-20. 2007
    ..We have performed a tomographic reconstruction, followed by averaging over approx. 150 individual reconstructions, of Drosophila 26S proteasomes suspended in a thin layer of amorphous ice...
  47. pmc Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution
    Stefan Bohn
    Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 107:20992-7. 2010
    ..An integrated model is presented which sheds light on the early steps of protein degradation by the 26S complex...
  48. ncbi request reprint Expression of an archaeal chaperonin in E. coli: formation of homo- (alpha, beta) and hetero-oligomeric (alpha+beta) thermosome complexes
    T Waldmann
    , Martinsried, Germany
    FEBS Lett 376:67-73. 1995
    ..The recombinant alpha-complex as well as the native thermosome could be reconstituted in vitro from their dissociated subunits in the presence of Mg-ATP...
  49. ncbi request reprint The role of tricorn protease and its aminopeptidase-interacting factors in cellular protein degradation
    N Tamura
    Max Planck Institut fur Biochemie, Martinsried, Germany
    Cell 95:637-48. 1998
    ..Therefore, it is quite likely that Tricorn also acts in vivo downstream of the proteasome and, in cooperation with its interacting factors, completes protein catabolic pathways...
  50. ncbi request reprint Capsids of tricorn protease studied by electron cryomicroscopy
    J Walz
    Department of Molecular Structural Biology, Max Planck Institut fur Biochemie, Martinsried, 82152, Germany
    J Struct Biol 128:65-8. 1999
    ..6 MDa. We have used electron cryomicroscopy to determine the structure of the Tricorn capsids to a resolution of 1.3 nm...
  51. ncbi request reprint Crystal structure of the beta-apical domain of the thermosome reveals structural plasticity in the protrusion region
    G Bosch
    Max Planck Institute for Biochemistry, Am Klopferspitz 18a, Martinsried bei Munchen, D 82152, Germany
    J Mol Biol 301:19-25. 2000
    ..Sequence variations in the protrusion regions that are found in the eukaryotic TRiC/CCT subunits may provide different structural propensities and hence serve different roles in substrate recognition...
  52. pmc Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography
    Friedrich Förster
    Abteilung für Molekulare Strukturbiologie, Max Planck Institut fur Biochemie, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 102:4729-34. 2005
    ..This study thus provides 3D structural information regarding the prefusion conformation of an intact unstained retrovirus surface protein...
  53. pmc Identification of macromolecular complexes in cryoelectron tomograms of phantom cells
    Achilleas S Frangakis
    Max Planck Institut fur Biochemie, Molekulare Strukturbiologie, Am Klopferspitz 18a, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 99:14153-8. 2002
    ..At the current resolution of approximately 4 nm, macromolecules in the size range of 0.5-1 MDa can be identified with good fidelity...
  54. pmc Molecular architecture and assembly mechanism of Drosophila tripeptidyl peptidase II
    Beate Rockel
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 102:10135-40. 2005
    ..Reciprocal interactions of the N-terminal part of subunits from neighboring strands are probably involved in the formation of the native quaternary structure, lending the TPPII spindle a stability higher than that of single strands...
  55. ncbi request reprint TOM software toolbox: acquisition and analysis for electron tomography
    Stephan Nickell
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    J Struct Biol 149:227-34. 2005
    ..TOM represents a new way of working with the electron microscope and can serve as the basis for future high-throughput applications...
  56. doi request reprint The three-dimensional organization of polyribosomes in intact human cells
    Florian Brandt
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Mol Cell 39:560-9. 2010
    ..The distinct neighbor orientations found in situ resemble configurations of bacterial polysomes in vitro, indicating a conserved supramolecular organization with implications for nascent polypeptide folding...
  57. ncbi request reprint Automated segmentation of electron tomograms for a quantitative description of actin filament networks
    Alexander Rigort
    Max Planck Institute of Biochemistry, Department of Structural Biology, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Struct Biol 177:135-44. 2012
    ....
  58. doi request reprint Structure and function of tripeptidyl peptidase II, a giant cytosolic protease
    Beate Rockel
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
    Biochim Biophys Acta 1824:237-45. 2012
    ..Here, we summarize our current knowledge about TPPII with a focus on structural aspects. This article is part of a Special Issue entitled: Proteolysis 50 years after the discovery of lysosome...
  59. doi request reprint Computer controlled cryo-electron microscopy--TOM² a software package for high-throughput applications
    Andreas Korinek
    Max Planck Institute of Biochemistry, Department of Molecular Structural Biology, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Struct Biol 175:394-405. 2011
    ..Its performance is demonstrated with a single particle analysis case study and with a batch tomography application...
  60. ncbi request reprint Insights into the molecular organization of the neuron by cryo-electron tomography
    Rubén Fernández-Busnadiego
    Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    J Electron Microsc (Tokyo) 60:S137-48. 2011
    ..Here, we will review these findings and discuss future directions towards the elucidation of the molecular landscape of the neuron...
  61. ncbi request reprint Quantitative proteome and transcriptome analysis of the archaeon Thermoplasma acidophilum cultured under aerobic and anaerobic conditions
    Na Sun
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Proteome Res 9:4839-50. 2010
    ....
  62. pmc Toward an integrated structural model of the 26S proteasome
    Friedrich Förster
    Department of Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
    Mol Cell Proteomics 9:1666-77. 2010
    ..These data allowed us to compute an atomic model for the CP-AAA-ATPase subcomplex. In addition to this atomic model, further subunits can be mapped approximately, which lets us hypothesize on the substrate path during its degradation...
  63. doi request reprint Micromachining tools and correlative approaches for cellular cryo-electron tomography
    Alexander Rigort
    Max Planck Institute of Biochemistry, Department of Molecular Structural Biology, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Struct Biol 172:169-79. 2010
    ..We also introduce a novel cryo-planing procedure as a method that could facilitate thinning of large areas of vitreous ice prior to cryo-fluorescence, FIB thinning, and cryo-electron tomography...
  64. ncbi request reprint New insights into the structural organization of eukaryotic and prokaryotic cytoskeletons using cryo-electron tomography
    Julia Kürner
    Department of Structural Biology, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    Exp Cell Res 301:38-42. 2004
    ..The application of cryo-ET to intact cells provides novel insights into the structure and the spatial organization of the cytoskeleton in prokaryotic and eukaryotic cells...
  65. ncbi request reprint Prospects of electron cryotomography to visualize macromolecular complexes inside cellular compartments: implications of crowding
    Kay Grünewald
    Department of Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Biophys Chem 100:577-91. 2003
    ..An example of the latter-a 5-fold symmetric particle is-given. Second, electron cryotomography offers an incisive probe to examine crowding in different cellular compartments...
  66. pmc Force spectroscopy of substrate molecules en route to the proteasome's active sites
    Mirjam Classen
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
    Biophys J 100:489-97. 2011
    ..These forces can be attributed to the translocation of substrate en route to the active sites that are harbored deep inside the proteasome...
  67. ncbi request reprint Electron tomography of vitreous sections from cultured mammalian cells
    Manuela Gruska
    Max Planck Institute for Biochemistry, Department of Structural Biology, Am Klopferspitz 18, D 82152 Martinsried, Germany
    J Struct Biol 161:384-92. 2008
    ..In some cases, ATP synthases could be identified without ambiguity. These findings confirm the feasibility of investigating the structural biology of mammalian cells in three dimensions and at a resolution of 6-8 nm...
  68. ncbi request reprint Rotary and unidirectional metal shadowing of VAT: localization of the substrate-binding domain
    B Rockel
    Abteilung Molekulare Strukturbiologie, , Am Klopferspitz 18a, 82152 Martinsried, Germany
    J Struct Biol 132:162-8. 2000
    ..Thus, this method appears to be well suited to study the conformational changes that occur during the functional cycle of the protein...
  69. ncbi request reprint Tricorn protease exists as an icosahedral supermolecule in vivo
    J Walz
    Abteilung Molekulare Strukturbiologie, Max Planck Institut fur Biochemie, Martinsried, Germany
    Mol Cell 1:59-65. 1997
    ..We suggest that the tricorn capsid, in addition to its intrinsic proteolytic activity, serves as the organizing center of a multienzyme complex...
  70. ncbi request reprint Tricorn protease in bacteria: characterization of the enzyme from Streptomyces coelicolor
    N Tamura
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
    Biol Chem 382:449-58. 2001
    ....
  71. ncbi request reprint Cloning and sequencing of the gene encoding the large (alpha-) subunit of the proteasome from Thermoplasma acidophilum
    P Zwickl
    Max Planck Institut fur Biochemie, Martinsried, Germany
    FEBS Lett 278:217-21. 1991
    ..The significant sequence similarity to the various subunits of eukaryotic proteasomes make it likely that proteasomal proteins are encoded by one gene family of ancient origin...
  72. ncbi request reprint ATP-induced structural change of the thermosome is temperature-dependent
    I Gutsche
    Max-Planck-Institute for Biochemistry, Am Klopferspitz 18a, , D-82152, Germany
    J Struct Biol 135:139-46. 2001
    ..Our data reveal an analogy between the ATPase cycles of the two groups of chaperonins and enable us to put forward a model of thermosome action...
  73. ncbi request reprint Proteomics analysis of Thermoplasma acidophilum with a focus on protein complexes
    Na Sun
    Department of Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152 Martinsried bei munchen, Germany
    Mol Cell Proteomics 6:492-502. 2007
    ..Although these proteins exhibit homology to known sequences, their structures, subunit compositions, and biological functions are not yet known...
  74. doi request reprint The native 3D organization of bacterial polysomes
    Florian Brandt
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried 82152, Germany
    Cell 136:261-71. 2009
    ....
  75. ncbi request reprint Dynamic organization of the actin system in the motile cells of Dictyostelium
    Till Bretschneider
    Max Planck Institut fur Biochemie, D 82152 Martinsried, Germany
    J Muscle Res Cell Motil 23:639-49. 2002
    ..We discuss the potential of electron tomography of vitrified cells to visualize actin networks in their native association with membranes...
  76. ncbi request reprint A visual approach to proteomics
    Stephan Nickell
    Max Planck Institute for Biochemistry, Department of Structural Biology, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Nat Rev Mol Cell Biol 7:225-30. 2006
    ..Visual proteomics' aims to complement and extend mass-spectrometry-based inventories, and to provide a quantitative description of the macromolecular interactions that underlie cellular functions...
  77. doi request reprint Maximum likelihood based classification of electron tomographic data
    Michael Stölken
    Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    J Struct Biol 173:77-85. 2011
    ..Application of our approach to cryo-electron tomographic data of ice-embedded thermosomes revealed distinct conformations that are in good agreement with results obtained by previous single particle studies...
  78. ncbi request reprint The beta-propeller domain of the trilobed protease from Pyrococcus furiosus reveals an open Velcro topology
    Jürgen Bosch
    Max Planck Institute for Biochemistry, Department of Molecular Structural Biology, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Acta Crystallogr D Biol Crystallogr 63:179-87. 2007
    ..Modelling of the intact TLP monomer suggests that this protease has an additional side entrance to its active site as in the DPP-IV or tricorn protease complexes...
  79. doi request reprint Visualizing cells at the nanoscale
    Andrew Leis
    Max Planck Institute of Biochemistry, Department of Molecular Structural Biology, Am Klopferspitz 18, D 82152 Martinsried, Germany
    Trends Biochem Sci 34:60-70. 2009
    ..The systematic and comprehensive interpretation of such tomograms will provide unprecedented insight into the molecular organization of cellular landscapes...
  80. ncbi request reprint The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC
    T Waldmann
    Max Planck Institut fur Biochemie, Martinsried, Germany
    Eur J Biochem 227:848-56. 1995
    ..These striking structural similarities confirm the proposition that all these molecules belong to a single protein family which is structurally and functionally related to the GroEL class of molecular chaperones...
  81. pmc Three-dimensional architecture of actin filaments in Listeria monocytogenes comet tails
    Marion Jasnin
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 110:20521-6. 2013
    ..We propose a mechanism for the initiation of comet tail assembly and two scenarios that occur either independently or in concert for the ensuing actin-based motility, both emphasizing the role of filament bundling. ..
  82. ncbi request reprint Proteasome assembly triggers a switch required for active-site maturation
    Susanne Witt
    Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried 82152, Germany
    Structure 14:1179-88. 2006
    ..These data support the proposed assembly-dependent activation model in which the S2-S3 loop acts as an activation switch...
  83. ncbi request reprint Thermoplasma acidophilum TAA43 is an archaeal member of the eukaryotic meiotic branch of AAA ATPases
    Leticia Santos
    Max Planck Institute of Biochemistry, Department of Molecular Structural Biology, D 82152 Martinsried, Germany
    Biol Chem 385:1105-11. 2004
    ..Interestingly, immunoprecipitation analysis with TAA43 specific antibodies found a fraction of native TAA43 associated with Thermoplasma ribosomal proteins...
  84. ncbi request reprint Specific orientation and two-dimensional crystallization of the proteasome at metal-chelating lipid interfaces
    Andreas Thess
    Abteilung Molekulare Strukturbiologie, Max Planck Institut fur Biochemie, 82152 Martinsried, Germany
    J Biol Chem 277:36321-8. 2002
    ....
  85. pmc Luminal particles within cellular microtubules
    Boyan K Garvalov
    Axonal Growth and Regeneration Group, Max Planck Institute of Neurobiology, 82152 Martinsried, Germany
    J Cell Biol 174:759-65. 2006
    ..A higher accumulation of particles was seen near the retracting plus ends of microtubules. The luminal particles were abundant in neurons, but were also observed in other cells, such as astrocytes and stem cells...
  86. pmc Whole cell cryo-electron tomography reveals distinct disassembly intermediates of vaccinia virus
    Marek Cyrklaff
    Department of Molecular Structural Biology, Max Planck Institute for Biochemistry, Martinsried, Germany
    PLoS ONE 2:e420. 2007
    ..Generally, this is the first study that employs whole cell cryo-ET to address structural details of pathogen-host cell interaction...
  87. pmc Energy filtered electron tomography of ice-embedded actin and vesicles
    R Grimm
    Max Planck Institut fur Biochemie, Molekulare Strukturbiologie, Martinsried, Germany
    Biophys J 72:482-9. 1997
    ..Actin filaments located on the outside usually associate with the vesicle membrane...
  88. ncbi request reprint Primary structure of the thermosome from Thermoplasma acidophilum
    T Waldmann
    Max Planck Institut fur Biochemie, Martinsried, Germany
    Biol Chem Hoppe Seyler 376:119-26. 1995
    ....
  89. ncbi request reprint The Thermoplasma acidophilum rpl15 gene encodes a homologue of eukaryotic ribosomal proteins L15/YL10
    P Zwickl
    Max Planck Institut fur Biochemie, Martinsried, Germany
    Biochem Biophys Res Commun 209:684-8. 1995
    ..59. The RPL15 amino acid sequence shows significant similarity (> 35% identity) to the L15/YL10 proteins of various eukaryotes...
  90. ncbi request reprint Conformational rearrangements of an archaeal chaperonin upon ATPase cycling
    I Gutsche
    Max Planck Institute for Biochemistry, Martinsried bei Munchen, D 82152, Germany
    Curr Biol 10:405-8. 2000
    ..The same closure can be triggered by the crystallization buffer. Thus, the allosteric regulation of group II chaperonins appears different from that of their group I counterparts...
  91. ncbi request reprint ATPase cycle of an archaeal chaperonin
    I Gutsche
    Max Planck Institute for Biochemistry, Am Klopferspitz 18a, Martinsried, D 82152, Germany
    J Mol Biol 300:187-96. 2000
    ..The effect of Mg(2+) and K(+) nucleotide cycling is documented. We conclude that archaeal chaperonins have unique allosteric properties and discuss them in the light of the mechanism established for the group I chaperonins...
  92. ncbi request reprint ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo-electron microscopy
    I Gutsche
    Max Planck Institute for Biochemistry, Am Klopferspitz 18a, D 82152, Martinsried, Germany
    FEBS Lett 477:278-82. 2000
    ..Here, we show that the conformation of the native alphabeta-thermosome of Thermoplasma acidophilum in vitrified ice is strictly regulated by adenine nucleotides...
  93. pmc Toward detecting and identifying macromolecules in a cellular context: template matching applied to electron tomograms
    J Bohm
    Department of Molecular Structural Biology, Max Planck Institute for Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 97:14245-50. 2000
    ..This opens up exciting prospects for mapping the territorial distribution of macromolecules and for analyzing molecular interactions in situ...
  94. pmc Isolation and cloning of Omp alpha, a coiled-coil protein spanning the periplasmic space of the ancestral eubacterium Thermotoga maritima
    A M Engel
    Max Planck Institut fur Biochemie, Martinsried, Germany
    EMBO J 11:4369-78. 1992
    ....
  95. ncbi request reprint Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum
    V Pamnani
    Max Planck Institut fur Biochemie, Martinsried, Germany
    FEBS Lett 404:263-8. 1997
    ..Electron microscopy shows the purified protein to form single and double homo-hexameric rings. Although the symmetry is different, the appearance of the complexes formed of two rings resembles the 20S proteasome and Hsp60/GroEL...
  96. ncbi request reprint Cryo-electron tomography of neurospora mitochondria
    D Nicastro
    Abteilung Molekulare Strukturbiologie, Max Planck Institut fur Biochemie, Martinsried, 82152, Germany
    J Struct Biol 129:48-56. 2000
    ..This indicates that it is a realistic goal to achieve "molecular resolution" with rather large biological specimens in the near future, ultimately allowing the identification and localization of macromolecules in their cellular context...
  97. ncbi request reprint Primary structure of a multimeric protein, homologous to the PEP-utilizing enzyme family and isolated from a hyperthermophilic archaebacterium
    C Cicicopol
    Max Planck Institut fur Biochemie, Martinsried, Germany
    FEBS Lett 356:345-50. 1994
    ..Its homomultimeric organisation differs from the typically dimeric structure of its eubacterial and eukaryotic counterparts...
  98. ncbi request reprint Tricorn protease (TRI) interacting factor 1 from Thermoplasma acidophilum is a proline iminopeptidase
    T Tamura
    Max Planck Institute for Biochemistry, Martinsried, Germany
    FEBS Lett 398:101-5. 1996
    ..Experiments with inactive mutant PIPs indicate that the activities elicited by interacting with TRI are contributed by PIP...
  99. ncbi request reprint Subunit topology of the Rhodococcus proteasome
    F Zühl
    Max Planck Institute for Biochemistry, Martinsreid, Germany
    FEBS Lett 400:83-90. 1997
    ..The experiments further indicate that the assembly pathways of the Rhodococcus and of the Thermoplasma proteasome differ in some important details...
  100. ncbi request reprint Determination of the inelastic mean free path in ice by examination of tilted vesicles and automated most probable loss imaging
    R Grimm
    Max Planck Institut fur Biochemie, Martinsried, Germany
    Ultramicroscopy 63:169-79. 1996
    ..Even at large ice thicknesses zero-loss filtering always gives better image contrast. Most probable loss imaging can only help where there is no intensity in the zero-loss image, at very large thicknesses (lambda > 8)...
  101. ncbi request reprint Proteasome: from structure to function
    D Stock
    Abteilung Strukturforschung, Max Planck Institut fur Biochemie, Martinsried, Germany
    Curr Opin Biotechnol 7:376-85. 1996
    ..Close relationships to a number of other amino-terminal hydrolases have emerged, making the proteasomal subunits the prototype of this newly discovered structural superfamily...