Journal: Acta Crystallographica Section D: Biological Crystallography

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Abbreviation

Acta crystallogr., D, Biol. crystallogr.

Publisher

Wiley-Blackwell

Journal Volumes

ISSN

0907-4449
1399-0047

Description

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Publications 1 - 10 of 16
  • Alonso-García, Noelia; García-Rubio, Inés; Manso, José A.; et al. (2015)
    Acta Crystallographica Section D: Biological Crystallography
    Integrin α6β4 is a major component of hemidesmosomes that mediate the stable anchorage of epithelial cells to the underlying basement membrane. Integrin α6β4 has also been implicated in cell proliferation and migration and in carcinoma progression. The third and fourth fibronectin type III domains (FnIII-3,4) of integrin β4 mediate binding to the hemidesmosomal proteins BPAG1e and BPAG2, and participate in signalling. Here, it is demonstrated that X-ray crystallography, small-angle X-ray scattering and double electron–electron resonance (DEER) complement each other to solve the structure of the FnIII-3,4 region. The crystal structures of the individual FnIII-3 and FnIII-4 domains were solved and the relative arrangement of the FnIII domains was elucidated by combining DEER with site-directed spin labelling. Multiple structures of the interdomain linker were modelled by Monte Carlo methods complying with DEER constraints, and the final structures were selected against experimental scattering data. FnIII-3,4 has a compact and cambered flat structure with an evolutionary conserved surface that is likely to correspond to a protein-interaction site. Finally, this hybrid method is of general application for the study of other macromolecules and complexes.
  • Manjasetty, B.A.; Hennecke, J.; Glockshuber, R.; et al. (2004)
    Acta Crystallographica Section D: Biological Crystallography
  • Jenni, Simon; Ban, Nenad (2009)
    Acta Crystallographica Section D: Biological Crystallography
    The recent high-resolution structures of fungal fatty acid synthase (FAS) have provided new insights into the principles of fatty acid biosynthesis by large multifunctional enzymes. The crystallographic phase problem for the 2.6 MDa fungal FAS was initially solved to 5 Å resolution using two crystal forms from Thermomyces lanuginosus. Monoclinic crystals in space group P21 were obtained from orthorhombic crystals in space group P212121 by dehydration. Here, it is shown how this space-group transition induced imperfect pseudo-merohedral twinning in the monoclinic crystal, giving rise to a Moiré pattern-like interference of the two twin-related reciprocal lattices. The strategy for processing the twinned diffraction images and obtaining a quantitative analysis is presented. The twinning is also related to the packing of the molecules in the two crystal forms, which was derived from self-rotation function analysis and molecular-replacement solutions using a low-resolution electron microscopy map as a search model.
  • Barandun, Luzi J.; Immekus, Florian; Kohler, Philipp C.; et al. (2013)
    Acta Crystallographica Section D: Biological Crystallography
  • Citations in supplementary material
    Item type: Other Journal Item
    Weiss, Manfred S.; Einspahr, Howard; Baker, Edward N.; et al. (2010)
    Acta Crystallographica Section D: Biological Crystallography
  • Sargent, David F.; Richmond, Timothy J. (2004)
    Acta Crystallographica Section D: Biological Crystallography
  • Dworkowski, Florian S.N.; Hough, Michael A.; Pompidor, Guillaume; et al. (2015)
    Acta Crystallographica Section D: Biological Crystallography
    Combining macromolecular crystallography with in crystallo micro-spectrophotometry yields valuable complementary information on the sample, including the redox states of metal cofactors, the identification of bound ligands and the onset and strength of undesired photochemistry, also known as radiation damage. However, the analysis and processing of the resulting data differs significantly from the approaches used for solution spectrophotometric data. The varying size and shape of the sample, together with the suboptimal sample environment, the lack of proper reference signals and the general influence of the X-ray beam on the sample have to be considered and carefully corrected for. In the present article, how to characterize and treat these sample-dependent artefacts in a reproducible manner is discussed and the SLS-APE in situ, in crystallo optical spectroscopy data-analysis toolbox is demonstrated.
  • Portuondo-Campa, E.; Schenkl, S.; Dolder, M.; et al. (2006)
    Acta Crystallographica Section D: Biological Crystallography
  • Ellermann, Manuel; Lerner, Christian; Burgy, Guillaume; et al. (2012)
    Acta Crystallographica Section D: Biological Crystallography
  • Korndoerfer, Ingo P.; Kanitz, Alexander; Danzer, Josef; et al. (2008)
    Acta Crystallographica Section D: Biological Crystallography
Publications 1 - 10 of 16